Intrinsically Disordered Protein TEX264 Mediates ER-phagy
Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions (LIRs) that bind to autophagosomal LC3 and GABARAP family proteins. Here, we performed a differential interactome screen using wild-type LC3B...
Saved in:
Published in | Molecular cell Vol. 74; no. 5; pp. 909 - 921.e6 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
06.06.2019
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions (LIRs) that bind to autophagosomal LC3 and GABARAP family proteins. Here, we performed a differential interactome screen using wild-type LC3B and a LIR recognition-deficient mutant and identified TEX264 as a receptor for autophagic degradation of the endoplasmic reticulum (ER-phagy). TEX264 is an ER protein with a single transmembrane domain and a LIR motif. TEX264 interacts with LC3 and GABARAP family proteins more efficiently and is expressed more ubiquitously than previously known ER-phagy receptors. ER-phagy is profoundly blocked by deletion of TEX264 alone and almost completely by additional deletion of FAM134B and CCPG1. A long intrinsically disordered region of TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomal membranes independently of its amino acid sequence. These results suggest that TEX264 is a major ER-phagy receptor.
[Display omitted]
•TEX264 was identified by a differential LC3B-interactome screen•TEX264 is an ER transmembrane protein with an LC3-interacting region•TEX264 acts as a major receptor for autophagic degradation of the ER (ER-phagy)•A disordered region in TEX264 bridges the gap between the ER and autophagosomes
Macroautophagy can selectively recognize and degrade organelles such as the ER. Chino et al. identified TEX264 as a receptor for autophagic degradation of the ER (ER-phagy). A long intrinsically disordered region in TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomes. |
---|---|
AbstractList | Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions (LIRs) that bind to autophagosomal LC3 and GABARAP family proteins. Here, we performed a differential interactome screen using wild-type LC3B and a LIR recognition-deficient mutant and identified TEX264 as a receptor for autophagic degradation of the endoplasmic reticulum (ER-phagy). TEX264 is an ER protein with a single transmembrane domain and a LIR motif. TEX264 interacts with LC3 and GABARAP family proteins more efficiently and is expressed more ubiquitously than previously known ER-phagy receptors. ER-phagy is profoundly blocked by deletion of TEX264 alone and almost completely by additional deletion of FAM134B and CCPG1. A long intrinsically disordered region of TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomal membranes independently of its amino acid sequence. These results suggest that TEX264 is a major ER-phagy receptor.
[Display omitted]
•TEX264 was identified by a differential LC3B-interactome screen•TEX264 is an ER transmembrane protein with an LC3-interacting region•TEX264 acts as a major receptor for autophagic degradation of the ER (ER-phagy)•A disordered region in TEX264 bridges the gap between the ER and autophagosomes
Macroautophagy can selectively recognize and degrade organelles such as the ER. Chino et al. identified TEX264 as a receptor for autophagic degradation of the ER (ER-phagy). A long intrinsically disordered region in TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomes. Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions (LIRs) that bind to autophagosomal LC3 and GABARAP family proteins. Here, we performed a differential interactome screen using wild-type LC3B and a LIR recognition-deficient mutant and identified TEX264 as a receptor for autophagic degradation of the endoplasmic reticulum (ER-phagy). TEX264 is an ER protein with a single transmembrane domain and a LIR motif. TEX264 interacts with LC3 and GABARAP family proteins more efficiently and is expressed more ubiquitously than previously known ER-phagy receptors. ER-phagy is profoundly blocked by deletion of TEX264 alone and almost completely by additional deletion of FAM134B and CCPG1. A long intrinsically disordered region of TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomal membranes independently of its amino acid sequence. These results suggest that TEX264 is a major ER-phagy receptor. |
Author | Chino, Haruka Hatta, Tomohisa Mizushima, Noboru Natsume, Tohru |
Author_xml | – sequence: 1 givenname: Haruka surname: Chino fullname: Chino, Haruka organization: Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan – sequence: 2 givenname: Tomohisa surname: Hatta fullname: Hatta, Tomohisa organization: Molecular Profiling Research Center for Drug Discovery (molprof), National Institute of Advanced Industrial Science and Technology (AIST), Tokyo 135-0064, Japan – sequence: 3 givenname: Tohru surname: Natsume fullname: Natsume, Tohru organization: Molecular Profiling Research Center for Drug Discovery (molprof), National Institute of Advanced Industrial Science and Technology (AIST), Tokyo 135-0064, Japan – sequence: 4 givenname: Noboru surname: Mizushima fullname: Mizushima, Noboru email: nmizu@m.u-tokyo.ac.jp organization: Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31006538$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kEtLA0EQhAeJGBP9ByJ79LJrz2NfF0Fi1EBEkQjeht2ZXp2wjzizEfLvnbDRo9DQfajqor4JGbVdi4RcUIgo0OR6HTVdrbCOGNA8Au6HH5FTCnkaCpqI0eFmaRKPycS5NQAVcZafkDGnAEnMs1OSL9remtYZVdT1LrgzrrMaLergxXY9mjZYzd9ZIoIn1Kbo0QXz13DzWXzszshxVdQOzw97St7u56vZY7h8fljMbpehEqnow6JgkCaV0LkGxDLOlFY-W5UYJ5SWqIAxmmWpV4FAUVY8Bq6ZKoGWGhLBp-Rq-Lux3dcWXS8b43zvumix2zrp7Sz1fTnzUjFIle2cs1jJjTVNYXeSgtxDk2s5QJN7aBK4H-5tl4eEbdmg_jP9UvKCm0GAvue3QSudMtgqj8Si6qXuzP8JP106f1g |
CitedBy_id | crossref_primary_10_1016_j_jmb_2019_05_012 crossref_primary_10_1146_annurev_cellbio_100818_125300 crossref_primary_10_1016_j_jbc_2023_105282 crossref_primary_10_1016_j_jmb_2019_05_010 crossref_primary_10_2183_pjab_96_001 crossref_primary_10_1080_15548627_2022_2119350 crossref_primary_10_1083_jcb_202302067 crossref_primary_10_1016_j_tibs_2019_11_006 crossref_primary_10_15252_embr_202052289 crossref_primary_10_3389_fcell_2022_844481 crossref_primary_10_1038_s41598_020_60346_2 crossref_primary_10_1038_s41467_022_35501_0 crossref_primary_10_15252_embj_2020107240 crossref_primary_10_3390_biomedicines9080939 crossref_primary_10_1016_j_jjcc_2019_09_019 crossref_primary_10_1016_j_neuron_2022_01_017 crossref_primary_10_1016_j_mcn_2023_103822 crossref_primary_10_1186_s12983_020_00366_w crossref_primary_10_1007_s12975_022_01090_9 crossref_primary_10_1002_jcp_30377 crossref_primary_10_15252_embj_2023113625 crossref_primary_10_1111_jcmm_17300 crossref_primary_10_3389_fcell_2021_684526 crossref_primary_10_1016_j_jmb_2020_01_015 crossref_primary_10_1016_j_yexcr_2020_112276 crossref_primary_10_1111_febs_15031 crossref_primary_10_1016_j_jmb_2020_01_017 crossref_primary_10_3389_fonc_2022_997235 crossref_primary_10_4103_NRR_NRR_D_23_00995 crossref_primary_10_1038_s41467_019_12991_z crossref_primary_10_15252_embj_2023114272 crossref_primary_10_1111_febs_15824 crossref_primary_10_15252_embj_2019103649 crossref_primary_10_1111_cas_15112 crossref_primary_10_3389_fcell_2019_00373 crossref_primary_10_1016_j_devcel_2021_02_010 crossref_primary_10_1091_mbc_E22_09_0432 crossref_primary_10_1016_j_tcb_2020_02_001 crossref_primary_10_3389_fnins_2020_00090 crossref_primary_10_1083_jcb_201906047 crossref_primary_10_1038_s41467_024_47440_z crossref_primary_10_1016_j_devcel_2020_03_018 crossref_primary_10_1038_s41586_020_2446_y crossref_primary_10_7554_eLife_58396 crossref_primary_10_3390_cells10123337 crossref_primary_10_1038_s41392_023_01603_4 crossref_primary_10_1007_s00018_022_04585_8 crossref_primary_10_1016_j_devcel_2021_02_008 crossref_primary_10_1038_s41467_023_44101_5 crossref_primary_10_3390_cells10092328 crossref_primary_10_1002_bies_202000212 crossref_primary_10_3390_cells12081134 crossref_primary_10_1016_j_jmb_2024_168472 crossref_primary_10_1038_s41580_022_00542_2 crossref_primary_10_1038_s41419_024_06449_4 crossref_primary_10_1016_j_canlet_2024_216846 crossref_primary_10_1089_ars_2022_0202 crossref_primary_10_1080_14786419_2019_1690485 crossref_primary_10_1016_j_bbamcr_2019_118627 crossref_primary_10_3389_fmolb_2021_804097 crossref_primary_10_1080_15548627_2021_1872886 crossref_primary_10_1038_s41467_021_21715_1 crossref_primary_10_1126_sciadv_abi6582 crossref_primary_10_3390_pathogens12040629 crossref_primary_10_1016_j_tibs_2020_12_013 crossref_primary_10_1073_pnas_2315550121 crossref_primary_10_1016_j_isci_2020_101105 crossref_primary_10_3390_cells10102752 crossref_primary_10_1126_science_aau9263 crossref_primary_10_1371_journal_pone_0232645 crossref_primary_10_1002_1873_3468_13571 crossref_primary_10_1016_j_tcb_2022_08_006 crossref_primary_10_1016_j_devcel_2023_04_015 crossref_primary_10_1371_journal_pone_0239153 crossref_primary_10_1016_j_semcancer_2020_03_010 crossref_primary_10_1080_15384101_2023_2249302 crossref_primary_10_1038_s41586_023_06657_6 crossref_primary_10_1016_j_molcel_2020_05_002 crossref_primary_10_1016_j_jmb_2024_168691 crossref_primary_10_1016_j_molcel_2019_10_019 crossref_primary_10_1021_acs_analchem_3c02016 crossref_primary_10_1038_s41467_020_17163_y crossref_primary_10_1088_2399_1984_abfb7c crossref_primary_10_3390_ijms22042078 crossref_primary_10_1002_1873_3468_14433 crossref_primary_10_1016_j_celrep_2023_112286 crossref_primary_10_1016_j_mam_2021_100973 crossref_primary_10_15252_embr_202254801 crossref_primary_10_1091_mbc_E21_10_0505 crossref_primary_10_1016_j_fct_2023_113793 crossref_primary_10_3390_cells8091071 crossref_primary_10_1016_j_molcel_2022_08_008 crossref_primary_10_1038_s41467_021_23599_7 crossref_primary_10_1111_bcpt_13869 crossref_primary_10_1016_j_redox_2023_102943 crossref_primary_10_1016_j_lfs_2023_121705 crossref_primary_10_1016_j_ymthe_2022_04_022 crossref_primary_10_15252_embj_2019102586 crossref_primary_10_1016_j_bbalip_2021_159020 crossref_primary_10_1093_lifemedi_lnac043 crossref_primary_10_1080_15548627_2023_2165759 crossref_primary_10_1016_j_celrep_2023_113480 crossref_primary_10_1016_j_jmb_2019_10_013 crossref_primary_10_1038_s41568_021_00344_2 crossref_primary_10_1016_j_tcb_2022_04_006 crossref_primary_10_1038_s41422_023_00905_0 crossref_primary_10_3390_biomedicines10030707 crossref_primary_10_1038_s41467_020_15000_w crossref_primary_10_15252_embr_202357758 crossref_primary_10_1016_j_devcel_2021_03_005 crossref_primary_10_1186_s12943_024_01934_y crossref_primary_10_1016_j_cophys_2022_100613 crossref_primary_10_1080_15548627_2021_1968228 crossref_primary_10_1016_j_jaccao_2023_05_009 crossref_primary_10_1007_s00401_021_02347_7 crossref_primary_10_1016_j_ceb_2022_102084 crossref_primary_10_1016_j_molcel_2022_02_018 crossref_primary_10_1016_j_jmb_2023_168144 crossref_primary_10_1091_mbc_E21_10_0526 crossref_primary_10_1016_j_cell_2023_08_008 crossref_primary_10_3390_cells11071086 crossref_primary_10_1080_19491034_2023_2299632 crossref_primary_10_3389_fnins_2020_00048 crossref_primary_10_3389_fmolb_2022_930223 crossref_primary_10_1101_cshperspect_a041256 crossref_primary_10_3389_fonc_2020_619727 crossref_primary_10_1038_s41467_023_39172_3 crossref_primary_10_3390_cells10102711 crossref_primary_10_15252_embj_2019102608 crossref_primary_10_1038_s41401_023_01139_x crossref_primary_10_1080_15548627_2019_1646540 crossref_primary_10_15252_embj_2020105696 crossref_primary_10_3389_fcell_2023_1156152 crossref_primary_10_1038_s44318_024_00131_3 crossref_primary_10_3389_fimmu_2022_842077 crossref_primary_10_1039_D0CS00913J crossref_primary_10_3389_fmicb_2022_889835 crossref_primary_10_1016_j_molcel_2019_09_005 crossref_primary_10_1080_15548627_2024_2319901 crossref_primary_10_1016_j_jcmgh_2024_02_006 crossref_primary_10_1016_j_chembiol_2020_02_005 crossref_primary_10_1016_j_cell_2020_02_017 crossref_primary_10_1016_j_devcel_2020_06_033 crossref_primary_10_3389_fphar_2020_01141 crossref_primary_10_1083_jcb_202201068 crossref_primary_10_1155_2020_8865611 crossref_primary_10_1080_15548627_2024_2347103 crossref_primary_10_3390_cells9112349 crossref_primary_10_1038_s41467_021_21874_1 crossref_primary_10_7554_eLife_50034 crossref_primary_10_1016_j_tibs_2019_05_003 crossref_primary_10_1016_j_jmb_2019_07_016 crossref_primary_10_1111_febs_16986 crossref_primary_10_1038_s41467_022_31905_0 crossref_primary_10_1016_j_pbi_2021_102106 crossref_primary_10_1038_s41556_024_01356_4 crossref_primary_10_1007_s11010_023_04800_5 crossref_primary_10_1152_physrev_00038_2021 crossref_primary_10_1002_jnr_25225 crossref_primary_10_1021_acs_biochem_0c00969 crossref_primary_10_1016_j_phymed_2022_154361 crossref_primary_10_1172_JCI163584 crossref_primary_10_3390_ijms24032749 crossref_primary_10_1021_acschemneuro_1c00818 crossref_primary_10_7554_eLife_51918 crossref_primary_10_1080_15548627_2021_1965711 crossref_primary_10_3390_ijms242015036 crossref_primary_10_1007_s41048_020_00113_y crossref_primary_10_1038_s41586_020_2992_3 crossref_primary_10_1038_s41598_021_01123_7 crossref_primary_10_1080_15548627_2020_1783118 crossref_primary_10_1016_j_jmb_2019_06_031 crossref_primary_10_1016_j_tibs_2020_07_006 crossref_primary_10_3390_plants9121771 crossref_primary_10_3389_fcell_2020_00090 crossref_primary_10_1016_j_celrep_2024_114255 crossref_primary_10_1038_s41419_022_04813_w crossref_primary_10_1155_2022_4304419 crossref_primary_10_3389_fcell_2021_771353 crossref_primary_10_1038_s41587_022_01539_0 crossref_primary_10_1146_annurev_cellbio_120219_035530 crossref_primary_10_15252_embr_202255192 crossref_primary_10_1360_TB_2022_0877 crossref_primary_10_1016_j_molcel_2020_07_019 crossref_primary_10_1080_15548627_2020_1827780 crossref_primary_10_1146_annurev_biochem_013118_111603 crossref_primary_10_1111_febs_14932 crossref_primary_10_3389_fcell_2020_00420 crossref_primary_10_3390_ijms21103468 crossref_primary_10_1161_JAHA_122_029103 crossref_primary_10_1126_sciadv_abo1215 crossref_primary_10_1016_j_tcb_2024_01_011 crossref_primary_10_1038_s41598_024_53874_8 crossref_primary_10_1073_pnas_1912222116 crossref_primary_10_1002_jcp_30836 crossref_primary_10_1073_pnas_2020215118 crossref_primary_10_1073_pnas_2221929120 crossref_primary_10_1016_j_yexcr_2020_112417 crossref_primary_10_1016_j_jprot_2020_104072 crossref_primary_10_1038_s41418_019_0444_0 crossref_primary_10_1177_10738584241232963 crossref_primary_10_1038_s41586_023_06089_2 crossref_primary_10_3390_membranes12050457 |
Cites_doi | 10.1093/emboj/19.21.5720 10.1016/S0301-472X(03)00260-1 10.1016/bs.ircmb.2017.07.001 10.1080/15548627.2015.1017178 10.1016/j.nbd.2010.08.015 10.1126/science.aaf4382 10.1038/ncb3423 10.1016/j.molcel.2014.03.009 10.1016/j.devcel.2017.02.016 10.1146/annurev-biochem-072711-164947 10.1042/EBC20170092 10.4161/auto.6.6.12709 10.1002/1873-3468.12641 10.1242/dev.152413 10.12688/f1000research.13968.1 10.1016/j.sbi.2008.10.002 10.1038/ncb2979 10.1042/EBC20170035 10.1016/j.chembiol.2011.05.013 10.1016/j.tcb.2017.01.001 10.1038/s41556-018-0037-z 10.1016/j.cell.2011.10.026 10.1042/bse0550051 10.1242/jcs.156034 10.1016/j.devcel.2017.11.024 10.4161/auto.7.9.15760 10.1242/jcs.217364 10.1016/j.devcel.2016.06.015 10.1111/tra.12243 10.1038/ng.464 10.1038/nrm3696 10.1242/jcs.126128 10.4238/2015.May.4.14 10.1093/bioinformatics/16.4.404 10.15252/embj.201695189 10.15252/embr.201643587 10.1016/j.febslet.2010.01.018 10.1016/S0014-5793(02)03622-0 10.1038/s41580-018-0003-4 10.4161/auto.6.2.11134 10.1038/nrm.2015.8 10.1038/nature10098 10.1247/csf.07011 10.7554/eLife.25555 10.1083/jcb.201804185 10.1016/j.neuron.2014.12.007 10.1042/BST20170354 10.1021/ac020018n 10.1002/gcc.22211 10.4161/auto.4451 10.1038/nature14506 10.1038/nmeth.3543 10.4161/auto.4590 10.3390/ijms18091865 10.1083/jcb.200604129 10.1016/j.tcb.2015.08.010 10.1074/jbc.M109.072389 10.1111/febs.13202 10.1038/nmeth.2019 10.1111/j.1365-2443.2008.01238.x 10.1021/bi036269n 10.1016/j.devcel.2016.09.001 10.1016/j.molcel.2016.09.037 10.1083/jcb.201804132 10.1007/s00018-017-2562-5 10.1126/science.aaf6136 10.1083/jcb.200712064 10.1038/embor.2013.168 10.1038/nature14498 |
ContentType | Journal Article |
Copyright | 2019 Elsevier Inc. Copyright © 2019 Elsevier Inc. All rights reserved. |
Copyright_xml | – notice: 2019 Elsevier Inc. – notice: Copyright © 2019 Elsevier Inc. All rights reserved. |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 |
DOI | 10.1016/j.molcel.2019.03.033 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1097-4164 |
EndPage | 921.e6 |
ExternalDocumentID | 10_1016_j_molcel_2019_03_033 31006538 S1097276519302576 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | --- --K -DZ -~X 0R~ 123 1~5 2WC 4.4 457 4G. 5RE 62- 6I. 7-5 AACTN AAEDW AAFTH AAIAV AAKRW AAKUH AALRI AAUCE AAVLU AAXUO ABJNI ABMAC ABMWF ABVKL ACGFO ACGFS ACNCT ADBBV ADEZE ADJPV AEFWE AENEX AEXQZ AFFNX AFTJW AGKMS AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ ASPBG AVWKF AZFZN BAWUL CS3 DIK DU5 E3Z EBS EJD F5P FCP FDB FEDTE FIRID HH5 HVGLF IH2 IHE IXB J1W JIG KQ8 L7B M3Z M41 N9A NCXOZ O-L O9- OK1 P2P RCE RIG ROL RPZ SDG SES SSZ TR2 WQ6 ZA5 0SF AAEDT AAHBH AAMRU ADVLN AKAPO AKRWK CGR CUY CVF ECM EIF NPM .55 .GJ 29M 3O- 53G 5VS AAIKJ AAQFI AAQXK AAYXX ADMUD AGHFR CITATION FGOYB HZ~ OZT R2- UHS X7M ZGI ZXP 7X8 |
ID | FETCH-LOGICAL-c474t-aa2076f4d9d0eeb58cdc065cbe5611bec022188720704e4bf3503d2cb01bd0643 |
IEDL.DBID | ABVKL |
ISSN | 1097-2765 |
IngestDate | Fri Aug 16 10:07:39 EDT 2024 Thu Sep 26 17:40:19 EDT 2024 Sat Sep 28 08:27:14 EDT 2024 Fri Feb 23 02:30:34 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 5 |
Keywords | organellar contact site intrinsically disordered region ER-phagy selective autophagy |
Language | English |
License | Copyright © 2019 Elsevier Inc. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c474t-aa2076f4d9d0eeb58cdc065cbe5611bec022188720704e4bf3503d2cb01bd0643 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | http://www.cell.com/article/S1097276519302576/pdf |
PMID | 31006538 |
PQID | 2212716432 |
PQPubID | 23479 |
ParticipantIDs | proquest_miscellaneous_2212716432 crossref_primary_10_1016_j_molcel_2019_03_033 pubmed_primary_31006538 elsevier_sciencedirect_doi_10_1016_j_molcel_2019_03_033 |
PublicationCentury | 2000 |
PublicationDate | 2019-06-06 |
PublicationDateYYYYMMDD | 2019-06-06 |
PublicationDate_xml | – month: 06 year: 2019 text: 2019-06-06 day: 06 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Molecular cell |
PublicationTitleAlternate | Mol Cell |
PublicationYear | 2019 |
Publisher | Elsevier Inc |
Publisher_xml | – name: Elsevier Inc |
References | Yamamoto, Fujioka, Suzuki, Noshiro, Suzuki, Kondo-Kakuta, Kimura, Hirano, Ando, Noda, Ohsumi (bib66) 2016; 38 Fregno, Molinari (bib9) 2018; 7 Mizushima, Komatsu (bib41) 2011; 147 Takayama, Matsuura, Itakura (bib62) 2017; 591 Kabeya, Mizushima, Ueno, Yamamoto, Kirisako, Noda, Kominami, Ohsumi, Yoshimori (bib21) 2000; 19 Itakura, Mizushima (bib19) 2010; 6 Phillips, Voeltz (bib50) 2016; 17 Søreng, Neufeld, Simonsen (bib60) 2018; 336 Khaminets, Behl, Dikic (bib26) 2016; 26 Kishi-Itakura, Koyama-Honda, Itakura, Mizushima (bib28) 2014; 127 Yoshii, Kuma, Akashi, Hara, Yamamoto, Kurikawa, Itakura, Tsukamoto, Shitara, Eishi, Mizushima (bib68) 2016; 39 Rogov, Stolz, Ravichandran, Rios-Szwed, Suzuki, Kniss, Löhr, Wakatsuki, Dötsch, Dikic (bib52) 2017; 18 Yoshii, Mizushima (bib67) 2017; 18 Hara, Takamura, Kishi, Iemura, Natsume, Guan, Mizushima (bib17) 2008; 181 Kitamura, Koshino, Shibata, Oki, Nakajima, Nosaka, Kumagai (bib29) 2003; 31 Schwanhäusser, Busse, Li, Dittmar, Schuchhardt, Wolf, Chen, Selbach (bib55) 2011; 473 Schindelin, Arganda-Carreras, Frise, Kaynig, Longair, Pietzsch, Preibisch, Rueden, Saalfeld, Schmid (bib54) 2012; 9 Slobodkin, Elazar (bib57) 2013; 55 Biazik, Ylä-Anttila, Vihinen, Jokitalo, Eskelinen (bib3) 2015; 11 Liu, Liu (bib38) 2015; 14 Smith, Wilkinson (bib58) 2017; 61 Gatica, Lahiri, Klionsky (bib12) 2018; 20 Kovács, Pálfia, Réz, Vellai, Kovács (bib31) 2007; 3 Pickrell, Youle (bib51) 2015; 85 Nishimura, Tamura, Kono, Shimanaka, Arai, Yamamoto, Mizushima (bib46) 2017; 36 Gan, Peng, Nagy, Alcaraz, Gu, Guan (bib11) 2006; 175 Shin, Brangwynne (bib56) 2017; 357 Deng, Purtell, Lachance, Wold, Chen, Yue (bib5) 2017; 27 Smith, Harley, Kemp, Wills, Lee, Arends, von Kriegsheim, Behrends, Wilkinson (bib59) 2018; 44 Anding, Baehrecke (bib2) 2017; 41 Loi, Fregno, Guerra, Molinari (bib39) 2018; 46 Hayashi-Nishino, Fujita, Noda, Yamaguchi, Yoshimori, Yamamoto (bib18) 2010; 6 Dikic, Elazar (bib6) 2018; 19 Grumati, Dikic, Stolz (bib16) 2018; 131 Dunker, Silman, Uversky, Sussman (bib7) 2008; 18 Liang, Lingeman, Ahmed, Corn (bib37) 2018; 217 Oldfield, Dunker (bib49) 2014; 83 Katayama, Kogure, Mizushima, Yoshimori, Miyawaki (bib24) 2011; 18 Birgisdottir, Lamark, Johansen (bib4) 2013; 126 Fumagalli, Noack, Bergmann, Cebollero, Pisoni, Fasana, Fregno, Galli, Loi, Soldà (bib10) 2016; 18 Allen, Toth, James, Ganley (bib1) 2013; 14 Gomes, Dikic (bib13) 2014; 54 Eskelinen, Reggiori, Baba, Kovács, Seglen (bib8) 2011; 7 Liang, Wang, Peng, Gan, Guan (bib36) 2010; 285 Noda, Ohsumi, Inagaki (bib48) 2010; 584 Kurth, Pamminger, Hennings, Soehendra, Huebner, Rotthier, Baets, Senderek, Topaloglu, Farrell (bib33) 2009; 41 Kimura, Noda, Yoshimori (bib27) 2007; 3 Saitoh, Nakano, Yamamoto, Yamaoka (bib53) 2002; 532 Kjaergaard, Kragelund (bib30) 2017; 74 McGuffin, Bryson, Jones (bib40) 2000; 16 Morita, Hama, Izume, Tamura, Ueno, Yamashita, Sakamaki, Mimura, Morishita, Shihoya (bib44) 2018; 217 Noda, Kumeta, Nakatogawa, Satoo, Adachi, Ishii, Fujioka, Ohsumi, Inagaki (bib47) 2008; 13 Tsuboyama, Koyama-Honda, Sakamaki, Koike, Morishita, Mizushima (bib63) 2016; 354 Uversky (bib64) 2015; 282 Jan, Vormer, Jongejan, Röling, Silber, de Rooij, Hamer, Repping, van Pelt (bib20) 2017; 144 Kralt, Carretta, Mari, Reggiori, Steen, Poolman, Veenhoff (bib32) 2015; 16 Zhou (bib69) 2004; 43 Katayama, Yamamoto, Mizushima, Yoshimori, Miyawaki (bib23) 2008; 33 Gotoh, Ichikawa, Arai, Chiku, Sakamoto, Fujimoto, Hiramoto, Nammo, Yasuda, Yoshida, Kanai (bib14) 2014; 53 Grumati, Morozzi, Hölper, Mari, Harwardt, Yan, Müller, Reggiori, Heilemann, Dikic (bib15) 2017; 6 Lamb, Yoshimori, Tooze (bib35) 2013; 14 Mochida, Oikawa, Kimura, Kirisako, Hirano, Ohsumi, Nakatogawa (bib42) 2015; 522 Kaizuka, Morishita, Hama, Tsukamoto, Matsui, Toyota, Kodama, Ishihara, Mizushima, Mizushima (bib22) 2016; 64 Moreno-Mateos, Vejnar, Beaudoin, Fernandez, Mis, Khokha, Giraldez (bib43) 2015; 12 Khaminets, Heinrich, Mari, Grumati, Huebner, Akutsu, Liebmann, Stolz, Nietzsche, Koch (bib25) 2015; 522 Natsume, Yamauchi, Nakayama, Shinkawa, Yanagida, Takahashi, Isobe (bib45) 2002; 74 Stolz, Ernst, Dikic (bib61) 2014; 16 Yamamoto, Simonsen (bib65) 2011; 43 Lamark, Svenning, Johansen (bib34) 2017; 61 31176531 - Trends Biochem Sci. 2019 Sep;44(9):731-733 31362563 - Autophagy. 2019 Oct;15(10):1677-1681 Stolz (10.1016/j.molcel.2019.03.033_bib61) 2014; 16 Khaminets (10.1016/j.molcel.2019.03.033_bib25) 2015; 522 Smith (10.1016/j.molcel.2019.03.033_bib59) 2018; 44 Birgisdottir (10.1016/j.molcel.2019.03.033_bib4) 2013; 126 Zhou (10.1016/j.molcel.2019.03.033_bib69) 2004; 43 Katayama (10.1016/j.molcel.2019.03.033_bib24) 2011; 18 Yoshii (10.1016/j.molcel.2019.03.033_bib67) 2017; 18 Moreno-Mateos (10.1016/j.molcel.2019.03.033_bib43) 2015; 12 Kralt (10.1016/j.molcel.2019.03.033_bib32) 2015; 16 Schwanhäusser (10.1016/j.molcel.2019.03.033_bib55) 2011; 473 Lamb (10.1016/j.molcel.2019.03.033_bib35) 2013; 14 Gotoh (10.1016/j.molcel.2019.03.033_bib14) 2014; 53 Anding (10.1016/j.molcel.2019.03.033_bib2) 2017; 41 Dikic (10.1016/j.molcel.2019.03.033_bib6) 2018; 19 Shin (10.1016/j.molcel.2019.03.033_bib56) 2017; 357 Smith (10.1016/j.molcel.2019.03.033_bib58) 2017; 61 Nishimura (10.1016/j.molcel.2019.03.033_bib46) 2017; 36 Lamark (10.1016/j.molcel.2019.03.033_bib34) 2017; 61 Gomes (10.1016/j.molcel.2019.03.033_bib13) 2014; 54 Liang (10.1016/j.molcel.2019.03.033_bib37) 2018; 217 Kishi-Itakura (10.1016/j.molcel.2019.03.033_bib28) 2014; 127 Yoshii (10.1016/j.molcel.2019.03.033_bib68) 2016; 39 Liang (10.1016/j.molcel.2019.03.033_bib36) 2010; 285 Hayashi-Nishino (10.1016/j.molcel.2019.03.033_bib18) 2010; 6 Gan (10.1016/j.molcel.2019.03.033_bib11) 2006; 175 Morita (10.1016/j.molcel.2019.03.033_bib44) 2018; 217 Kjaergaard (10.1016/j.molcel.2019.03.033_bib30) 2017; 74 Natsume (10.1016/j.molcel.2019.03.033_bib45) 2002; 74 Kabeya (10.1016/j.molcel.2019.03.033_bib21) 2000; 19 Loi (10.1016/j.molcel.2019.03.033_bib39) 2018; 46 Dunker (10.1016/j.molcel.2019.03.033_bib7) 2008; 18 Jan (10.1016/j.molcel.2019.03.033_bib20) 2017; 144 Kurth (10.1016/j.molcel.2019.03.033_bib33) 2009; 41 Mochida (10.1016/j.molcel.2019.03.033_bib42) 2015; 522 Katayama (10.1016/j.molcel.2019.03.033_bib23) 2008; 33 Uversky (10.1016/j.molcel.2019.03.033_bib64) 2015; 282 Deng (10.1016/j.molcel.2019.03.033_bib5) 2017; 27 Noda (10.1016/j.molcel.2019.03.033_bib48) 2010; 584 Søreng (10.1016/j.molcel.2019.03.033_bib60) 2018; 336 Saitoh (10.1016/j.molcel.2019.03.033_bib53) 2002; 532 Pickrell (10.1016/j.molcel.2019.03.033_bib51) 2015; 85 Eskelinen (10.1016/j.molcel.2019.03.033_bib8) 2011; 7 Noda (10.1016/j.molcel.2019.03.033_bib47) 2008; 13 Grumati (10.1016/j.molcel.2019.03.033_bib15) 2017; 6 Schindelin (10.1016/j.molcel.2019.03.033_bib54) 2012; 9 Itakura (10.1016/j.molcel.2019.03.033_bib19) 2010; 6 Fumagalli (10.1016/j.molcel.2019.03.033_bib10) 2016; 18 Mizushima (10.1016/j.molcel.2019.03.033_bib41) 2011; 147 Hara (10.1016/j.molcel.2019.03.033_bib17) 2008; 181 Phillips (10.1016/j.molcel.2019.03.033_bib50) 2016; 17 Slobodkin (10.1016/j.molcel.2019.03.033_bib57) 2013; 55 Allen (10.1016/j.molcel.2019.03.033_bib1) 2013; 14 Oldfield (10.1016/j.molcel.2019.03.033_bib49) 2014; 83 Khaminets (10.1016/j.molcel.2019.03.033_bib26) 2016; 26 Takayama (10.1016/j.molcel.2019.03.033_bib62) 2017; 591 Yamamoto (10.1016/j.molcel.2019.03.033_bib66) 2016; 38 Kitamura (10.1016/j.molcel.2019.03.033_bib29) 2003; 31 Fregno (10.1016/j.molcel.2019.03.033_bib9) 2018; 7 Biazik (10.1016/j.molcel.2019.03.033_bib3) 2015; 11 Liu (10.1016/j.molcel.2019.03.033_bib38) 2015; 14 Yamamoto (10.1016/j.molcel.2019.03.033_bib65) 2011; 43 Kaizuka (10.1016/j.molcel.2019.03.033_bib22) 2016; 64 Kovács (10.1016/j.molcel.2019.03.033_bib31) 2007; 3 Rogov (10.1016/j.molcel.2019.03.033_bib52) 2017; 18 Tsuboyama (10.1016/j.molcel.2019.03.033_bib63) 2016; 354 Grumati (10.1016/j.molcel.2019.03.033_bib16) 2018; 131 McGuffin (10.1016/j.molcel.2019.03.033_bib40) 2000; 16 Gatica (10.1016/j.molcel.2019.03.033_bib12) 2018; 20 Kimura (10.1016/j.molcel.2019.03.033_bib27) 2007; 3 |
References_xml | – volume: 6 start-page: 764 year: 2010 end-page: 776 ident: bib19 article-title: Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins publication-title: Autophagy contributor: fullname: Mizushima – volume: 18 start-page: E1865 year: 2017 ident: bib67 article-title: Monitoring and measuring autophagy publication-title: Int. J. Mol. Sci. contributor: fullname: Mizushima – volume: 18 start-page: 756 year: 2008 end-page: 764 ident: bib7 article-title: Function and structure of inherently disordered proteins publication-title: Curr. Opin. Struct. Biol. contributor: fullname: Sussman – volume: 3 start-page: 452 year: 2007 end-page: 460 ident: bib27 article-title: Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3 publication-title: Autophagy contributor: fullname: Yoshimori – volume: 532 start-page: 45 year: 2002 end-page: 51 ident: bib53 article-title: Lymphotoxin-beta receptor mediates NEMO-independent NF-kappaB activation publication-title: FEBS Lett. contributor: fullname: Yamaoka – volume: 336 start-page: 1 year: 2018 end-page: 92 ident: bib60 article-title: Membrane trafficking in autophagy publication-title: Int. Rev. Cell Mol. Biol. contributor: fullname: Simonsen – volume: 16 start-page: 135 year: 2015 end-page: 147 ident: bib32 article-title: Intrinsically disordered linker and plasma membrane-binding motif sort Ist2 and Ssy1 to junctions publication-title: Traffic contributor: fullname: Veenhoff – volume: 26 start-page: 6 year: 2016 end-page: 16 ident: bib26 article-title: Ubiquitin-dependent and independent signals in selective autophagy publication-title: Trends Cell Biol. contributor: fullname: Dikic – volume: 175 start-page: 121 year: 2006 end-page: 133 ident: bib11 article-title: Role of FIP200 in cardiac and liver development and its regulation of TNFalpha and TSC-mTOR signaling pathways publication-title: J. Cell Biol. contributor: fullname: Guan – volume: 20 start-page: 233 year: 2018 end-page: 242 ident: bib12 article-title: Cargo recognition and degradation by selective autophagy publication-title: Nat. Cell Biol. contributor: fullname: Klionsky – volume: 16 start-page: 495 year: 2014 end-page: 501 ident: bib61 article-title: Cargo recognition and trafficking in selective autophagy publication-title: Nat. Cell Biol. contributor: fullname: Dikic – volume: 19 start-page: 349 year: 2018 end-page: 364 ident: bib6 article-title: Mechanism and medical implications of mammalian autophagy publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Elazar – volume: 39 start-page: 116 year: 2016 end-page: 130 ident: bib68 article-title: Systemic analysis of Atg5-null mice rescued from neonatal lethality by transgenic ATG5 expression in neurons publication-title: Dev. Cell contributor: fullname: Mizushima – volume: 131 start-page: jcs217364 year: 2018 ident: bib16 article-title: ER-phagy at a glance publication-title: J. Cell Sci. contributor: fullname: Stolz – volume: 217 start-page: 3354 year: 2018 end-page: 3367 ident: bib37 article-title: Atlastins remodel the endoplasmic reticulum for selective autophagy publication-title: J. Cell Biol. contributor: fullname: Corn – volume: 43 start-page: 17 year: 2011 end-page: 28 ident: bib65 article-title: The elimination of accumulated and aggregated proteins: a role for aggrephagy in neurodegeneration publication-title: Neurobiol. Dis. contributor: fullname: Simonsen – volume: 11 start-page: 439 year: 2015 end-page: 451 ident: bib3 article-title: Ultrastructural relationship of the phagophore with surrounding organelles publication-title: Autophagy contributor: fullname: Eskelinen – volume: 41 start-page: 1179 year: 2009 end-page: 1181 ident: bib33 article-title: Mutations in FAM134B, encoding a newly identified Golgi protein, cause severe sensory and autonomic neuropathy publication-title: Nat. Genet. contributor: fullname: Farrell – volume: 44 start-page: 217 year: 2018 end-page: 232.e11 ident: bib59 article-title: CCPG1 is a non-canonical autophagy cargo receptor essential for ER-phagy and pancreatic ER proteostasis publication-title: Dev. Cell contributor: fullname: Wilkinson – volume: 14 start-page: 4557 year: 2015 end-page: 4565 ident: bib38 article-title: Novel bioinformatic identification of differentially expressed tissue-specific and cancer-related proteins from the Human Protein Atlas for biomarker discovery publication-title: Genet. Mol. Res. contributor: fullname: Liu – volume: 127 start-page: 4089 year: 2014 end-page: 4102 ident: bib28 article-title: Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells publication-title: J. Cell Sci. contributor: fullname: Mizushima – volume: 61 start-page: 609 year: 2017 end-page: 624 ident: bib34 article-title: Regulation of selective autophagy: the p62/SQSTM1 paradigm publication-title: Essays Biochem. contributor: fullname: Johansen – volume: 354 start-page: 1036 year: 2016 end-page: 1041 ident: bib63 article-title: The ATG conjugation systems are important for degradation of the inner autophagosomal membrane publication-title: Science contributor: fullname: Mizushima – volume: 64 start-page: 835 year: 2016 end-page: 849 ident: bib22 article-title: An autophagic flux probe that releases an internal control publication-title: Mol. Cell contributor: fullname: Mizushima – volume: 6 start-page: e25555 year: 2017 ident: bib15 article-title: Full length RTN3 regulates turnover of tubular endoplasmic reticulum via selective autophagy publication-title: eLife contributor: fullname: Dikic – volume: 61 start-page: 625 year: 2017 end-page: 635 ident: bib58 article-title: ER homeostasis and autophagy publication-title: Essays Biochem. contributor: fullname: Wilkinson – volume: 38 start-page: 86 year: 2016 end-page: 99 ident: bib66 article-title: The intrinsically disordered protein Atg13 mediates supramolecular assembly of autophagy initiation complexes publication-title: Dev. Cell contributor: fullname: Ohsumi – volume: 181 start-page: 497 year: 2008 end-page: 510 ident: bib17 article-title: FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells publication-title: J. Cell Biol. contributor: fullname: Mizushima – volume: 16 start-page: 404 year: 2000 end-page: 405 ident: bib40 article-title: The PSIPRED protein structure prediction server publication-title: Bioinformatics contributor: fullname: Jones – volume: 522 start-page: 359 year: 2015 end-page: 362 ident: bib42 article-title: Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus publication-title: Nature contributor: fullname: Nakatogawa – volume: 7 start-page: 454 year: 2018 ident: bib9 article-title: Endoplasmic reticulum turnover: ER-phagy and other flavors in selective and non-selective ER clearance publication-title: F1000Res. contributor: fullname: Molinari – volume: 31 start-page: 1007 year: 2003 end-page: 1014 ident: bib29 article-title: Retrovirus-mediated gene transfer and expression cloning: powerful tools in functional genomics publication-title: Exp. Hematol. contributor: fullname: Kumagai – volume: 473 start-page: 337 year: 2011 end-page: 342 ident: bib55 article-title: Global quantification of mammalian gene expression control publication-title: Nature contributor: fullname: Selbach – volume: 83 start-page: 553 year: 2014 end-page: 584 ident: bib49 article-title: Intrinsically disordered proteins and intrinsically disordered protein regions publication-title: Annu. Rev. Biochem. contributor: fullname: Dunker – volume: 6 start-page: 301 year: 2010 end-page: 303 ident: bib18 article-title: Electron tomography reveals the endoplasmic reticulum as a membrane source for autophagosome formation publication-title: Autophagy contributor: fullname: Yamamoto – volume: 9 start-page: 676 year: 2012 end-page: 682 ident: bib54 article-title: Fiji: an open-source platform for biological-image analysis publication-title: Nat. Methods contributor: fullname: Schmid – volume: 43 start-page: 2141 year: 2004 end-page: 2154 ident: bib69 article-title: Polymer models of protein stability, folding, and interactions publication-title: Biochemistry contributor: fullname: Zhou – volume: 85 start-page: 257 year: 2015 end-page: 273 ident: bib51 article-title: The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson’s disease publication-title: Neuron contributor: fullname: Youle – volume: 41 start-page: 10 year: 2017 end-page: 22 ident: bib2 article-title: Cleaning house: selective autophagy of organelles publication-title: Dev. Cell contributor: fullname: Baehrecke – volume: 144 start-page: 3659 year: 2017 end-page: 3673 ident: bib20 article-title: Unraveling transcriptome dynamics in human spermatogenesis publication-title: Development contributor: fullname: van Pelt – volume: 584 start-page: 1379 year: 2010 end-page: 1385 ident: bib48 article-title: Atg8-family interacting motif crucial for selective autophagy publication-title: FEBS Lett. contributor: fullname: Inagaki – volume: 17 start-page: 69 year: 2016 end-page: 82 ident: bib50 article-title: Structure and function of ER membrane contact sites with other organelles publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Voeltz – volume: 18 start-page: 1382 year: 2017 end-page: 1396 ident: bib52 article-title: Structural and functional analysis of the GABARAP interaction motif (GIM) publication-title: EMBO Rep. contributor: fullname: Dikic – volume: 147 start-page: 728 year: 2011 end-page: 741 ident: bib41 article-title: Autophagy: renovation of cells and tissues publication-title: Cell contributor: fullname: Komatsu – volume: 13 start-page: 1211 year: 2008 end-page: 1218 ident: bib47 article-title: Structural basis of target recognition by Atg8/LC3 during selective autophagy publication-title: Genes Cells contributor: fullname: Inagaki – volume: 74 start-page: 3205 year: 2017 end-page: 3224 ident: bib30 article-title: Functions of intrinsic disorder in transmembrane proteins publication-title: Cell. Mol. Life Sci. contributor: fullname: Kragelund – volume: 282 start-page: 1182 year: 2015 end-page: 1189 ident: bib64 article-title: Functional roles of transiently and intrinsically disordered regions within proteins publication-title: FEBS J. contributor: fullname: Uversky – volume: 18 start-page: 1042 year: 2011 end-page: 1052 ident: bib24 article-title: A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery publication-title: Chem. Biol. contributor: fullname: Miyawaki – volume: 14 start-page: 759 year: 2013 end-page: 774 ident: bib35 article-title: The autophagosome: origins unknown, biogenesis complex publication-title: Nat. Rev. Mol. Cell Biol. contributor: fullname: Tooze – volume: 74 start-page: 4725 year: 2002 end-page: 4733 ident: bib45 article-title: A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics publication-title: Anal. Chem. contributor: fullname: Isobe – volume: 53 start-page: 1018 year: 2014 end-page: 1032 ident: bib14 article-title: Comprehensive exploration of novel chimeric transcripts in clear cell renal cell carcinomas using whole transcriptome analysis publication-title: Genes Chromosomes Cancer contributor: fullname: Kanai – volume: 19 start-page: 5720 year: 2000 end-page: 5728 ident: bib21 article-title: LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing publication-title: EMBO J. contributor: fullname: Yoshimori – volume: 27 start-page: 491 year: 2017 end-page: 504 ident: bib5 article-title: Autophagy receptors and neurodegenerative diseases publication-title: Trends Cell Biol. contributor: fullname: Yue – volume: 18 start-page: 1173 year: 2016 end-page: 1184 ident: bib10 article-title: Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery publication-title: Nat. Cell Biol. contributor: fullname: Soldà – volume: 217 start-page: 3817 year: 2018 end-page: 3828 ident: bib44 article-title: Genome-wide CRISPR screen identifies publication-title: J. Cell Biol. contributor: fullname: Shihoya – volume: 55 start-page: 51 year: 2013 end-page: 64 ident: bib57 article-title: The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy publication-title: Essays Biochem. contributor: fullname: Elazar – volume: 3 start-page: 655 year: 2007 end-page: 662 ident: bib31 article-title: Sequestration revisited: integrating traditional electron microscopy, de novo assembly and new results publication-title: Autophagy contributor: fullname: Kovács – volume: 591 start-page: 1199 year: 2017 end-page: 1211 ident: bib62 article-title: Dissection of ubiquitinated protein degradation by basal autophagy publication-title: FEBS Lett. contributor: fullname: Itakura – volume: 14 start-page: 1127 year: 2013 end-page: 1135 ident: bib1 article-title: Loss of iron triggers PINK1/Parkin-independent mitophagy publication-title: EMBO Rep. contributor: fullname: Ganley – volume: 7 start-page: 935 year: 2011 end-page: 956 ident: bib8 article-title: Seeing is believing: the impact of electron microscopy on autophagy research publication-title: Autophagy contributor: fullname: Seglen – volume: 285 start-page: 3499 year: 2010 end-page: 3509 ident: bib36 article-title: Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration publication-title: J. Biol. Chem. contributor: fullname: Guan – volume: 46 start-page: 699 year: 2018 end-page: 706 ident: bib39 article-title: Eat it right: ER-phagy and recovER-phagy publication-title: Biochem. Soc. Trans. contributor: fullname: Molinari – volume: 33 start-page: 1 year: 2008 end-page: 12 ident: bib23 article-title: GFP-like proteins stably accumulate in lysosomes publication-title: Cell Struct. Funct. contributor: fullname: Miyawaki – volume: 54 start-page: 224 year: 2014 end-page: 233 ident: bib13 article-title: Autophagy in antimicrobial immunity publication-title: Mol. Cell contributor: fullname: Dikic – volume: 357 year: 2017 ident: bib56 article-title: Liquid phase condensation in cell physiology and disease publication-title: Science contributor: fullname: Brangwynne – volume: 36 start-page: 1719 year: 2017 end-page: 1735 ident: bib46 article-title: Autophagosome formation is initiated at phosphatidylinositol synthase-enriched ER subdomains publication-title: EMBO J. contributor: fullname: Mizushima – volume: 126 start-page: 3237 year: 2013 end-page: 3247 ident: bib4 article-title: The LIR motif - crucial for selective autophagy publication-title: J. Cell Sci. contributor: fullname: Johansen – volume: 522 start-page: 354 year: 2015 end-page: 358 ident: bib25 article-title: Regulation of endoplasmic reticulum turnover by selective autophagy publication-title: Nature contributor: fullname: Koch – volume: 12 start-page: 982 year: 2015 end-page: 988 ident: bib43 article-title: CRISPRscan: designing highly efficient sgRNAs for CRISPR-Cas9 targeting in vivo publication-title: Nat. Methods contributor: fullname: Giraldez – volume: 19 start-page: 5720 year: 2000 ident: 10.1016/j.molcel.2019.03.033_bib21 article-title: LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing publication-title: EMBO J. doi: 10.1093/emboj/19.21.5720 contributor: fullname: Kabeya – volume: 31 start-page: 1007 year: 2003 ident: 10.1016/j.molcel.2019.03.033_bib29 article-title: Retrovirus-mediated gene transfer and expression cloning: powerful tools in functional genomics publication-title: Exp. Hematol. doi: 10.1016/S0301-472X(03)00260-1 contributor: fullname: Kitamura – volume: 336 start-page: 1 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib60 article-title: Membrane trafficking in autophagy publication-title: Int. Rev. Cell Mol. Biol. doi: 10.1016/bs.ircmb.2017.07.001 contributor: fullname: Søreng – volume: 11 start-page: 439 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib3 article-title: Ultrastructural relationship of the phagophore with surrounding organelles publication-title: Autophagy doi: 10.1080/15548627.2015.1017178 contributor: fullname: Biazik – volume: 43 start-page: 17 year: 2011 ident: 10.1016/j.molcel.2019.03.033_bib65 article-title: The elimination of accumulated and aggregated proteins: a role for aggrephagy in neurodegeneration publication-title: Neurobiol. Dis. doi: 10.1016/j.nbd.2010.08.015 contributor: fullname: Yamamoto – volume: 357 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib56 article-title: Liquid phase condensation in cell physiology and disease publication-title: Science doi: 10.1126/science.aaf4382 contributor: fullname: Shin – volume: 18 start-page: 1173 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib10 article-title: Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery publication-title: Nat. Cell Biol. doi: 10.1038/ncb3423 contributor: fullname: Fumagalli – volume: 54 start-page: 224 year: 2014 ident: 10.1016/j.molcel.2019.03.033_bib13 article-title: Autophagy in antimicrobial immunity publication-title: Mol. Cell doi: 10.1016/j.molcel.2014.03.009 contributor: fullname: Gomes – volume: 41 start-page: 10 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib2 article-title: Cleaning house: selective autophagy of organelles publication-title: Dev. Cell doi: 10.1016/j.devcel.2017.02.016 contributor: fullname: Anding – volume: 83 start-page: 553 year: 2014 ident: 10.1016/j.molcel.2019.03.033_bib49 article-title: Intrinsically disordered proteins and intrinsically disordered protein regions publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-072711-164947 contributor: fullname: Oldfield – volume: 61 start-page: 625 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib58 article-title: ER homeostasis and autophagy publication-title: Essays Biochem. doi: 10.1042/EBC20170092 contributor: fullname: Smith – volume: 6 start-page: 764 year: 2010 ident: 10.1016/j.molcel.2019.03.033_bib19 article-title: Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins publication-title: Autophagy doi: 10.4161/auto.6.6.12709 contributor: fullname: Itakura – volume: 591 start-page: 1199 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib62 article-title: Dissection of ubiquitinated protein degradation by basal autophagy publication-title: FEBS Lett. doi: 10.1002/1873-3468.12641 contributor: fullname: Takayama – volume: 144 start-page: 3659 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib20 article-title: Unraveling transcriptome dynamics in human spermatogenesis publication-title: Development doi: 10.1242/dev.152413 contributor: fullname: Jan – volume: 7 start-page: 454 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib9 article-title: Endoplasmic reticulum turnover: ER-phagy and other flavors in selective and non-selective ER clearance publication-title: F1000Res. doi: 10.12688/f1000research.13968.1 contributor: fullname: Fregno – volume: 18 start-page: 756 year: 2008 ident: 10.1016/j.molcel.2019.03.033_bib7 article-title: Function and structure of inherently disordered proteins publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2008.10.002 contributor: fullname: Dunker – volume: 16 start-page: 495 year: 2014 ident: 10.1016/j.molcel.2019.03.033_bib61 article-title: Cargo recognition and trafficking in selective autophagy publication-title: Nat. Cell Biol. doi: 10.1038/ncb2979 contributor: fullname: Stolz – volume: 61 start-page: 609 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib34 article-title: Regulation of selective autophagy: the p62/SQSTM1 paradigm publication-title: Essays Biochem. doi: 10.1042/EBC20170035 contributor: fullname: Lamark – volume: 18 start-page: 1042 year: 2011 ident: 10.1016/j.molcel.2019.03.033_bib24 article-title: A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2011.05.013 contributor: fullname: Katayama – volume: 27 start-page: 491 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib5 article-title: Autophagy receptors and neurodegenerative diseases publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2017.01.001 contributor: fullname: Deng – volume: 20 start-page: 233 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib12 article-title: Cargo recognition and degradation by selective autophagy publication-title: Nat. Cell Biol. doi: 10.1038/s41556-018-0037-z contributor: fullname: Gatica – volume: 147 start-page: 728 year: 2011 ident: 10.1016/j.molcel.2019.03.033_bib41 article-title: Autophagy: renovation of cells and tissues publication-title: Cell doi: 10.1016/j.cell.2011.10.026 contributor: fullname: Mizushima – volume: 55 start-page: 51 year: 2013 ident: 10.1016/j.molcel.2019.03.033_bib57 article-title: The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy publication-title: Essays Biochem. doi: 10.1042/bse0550051 contributor: fullname: Slobodkin – volume: 127 start-page: 4089 year: 2014 ident: 10.1016/j.molcel.2019.03.033_bib28 article-title: Ultrastructural analysis of autophagosome organization using mammalian autophagy-deficient cells publication-title: J. Cell Sci. doi: 10.1242/jcs.156034 contributor: fullname: Kishi-Itakura – volume: 44 start-page: 217 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib59 article-title: CCPG1 is a non-canonical autophagy cargo receptor essential for ER-phagy and pancreatic ER proteostasis publication-title: Dev. Cell doi: 10.1016/j.devcel.2017.11.024 contributor: fullname: Smith – volume: 7 start-page: 935 year: 2011 ident: 10.1016/j.molcel.2019.03.033_bib8 article-title: Seeing is believing: the impact of electron microscopy on autophagy research publication-title: Autophagy doi: 10.4161/auto.7.9.15760 contributor: fullname: Eskelinen – volume: 131 start-page: jcs217364 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib16 article-title: ER-phagy at a glance publication-title: J. Cell Sci. doi: 10.1242/jcs.217364 contributor: fullname: Grumati – volume: 38 start-page: 86 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib66 article-title: The intrinsically disordered protein Atg13 mediates supramolecular assembly of autophagy initiation complexes publication-title: Dev. Cell doi: 10.1016/j.devcel.2016.06.015 contributor: fullname: Yamamoto – volume: 16 start-page: 135 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib32 article-title: Intrinsically disordered linker and plasma membrane-binding motif sort Ist2 and Ssy1 to junctions publication-title: Traffic doi: 10.1111/tra.12243 contributor: fullname: Kralt – volume: 41 start-page: 1179 year: 2009 ident: 10.1016/j.molcel.2019.03.033_bib33 article-title: Mutations in FAM134B, encoding a newly identified Golgi protein, cause severe sensory and autonomic neuropathy publication-title: Nat. Genet. doi: 10.1038/ng.464 contributor: fullname: Kurth – volume: 14 start-page: 759 year: 2013 ident: 10.1016/j.molcel.2019.03.033_bib35 article-title: The autophagosome: origins unknown, biogenesis complex publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm3696 contributor: fullname: Lamb – volume: 126 start-page: 3237 year: 2013 ident: 10.1016/j.molcel.2019.03.033_bib4 article-title: The LIR motif - crucial for selective autophagy publication-title: J. Cell Sci. doi: 10.1242/jcs.126128 contributor: fullname: Birgisdottir – volume: 14 start-page: 4557 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib38 article-title: Novel bioinformatic identification of differentially expressed tissue-specific and cancer-related proteins from the Human Protein Atlas for biomarker discovery publication-title: Genet. Mol. Res. doi: 10.4238/2015.May.4.14 contributor: fullname: Liu – volume: 16 start-page: 404 year: 2000 ident: 10.1016/j.molcel.2019.03.033_bib40 article-title: The PSIPRED protein structure prediction server publication-title: Bioinformatics doi: 10.1093/bioinformatics/16.4.404 contributor: fullname: McGuffin – volume: 36 start-page: 1719 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib46 article-title: Autophagosome formation is initiated at phosphatidylinositol synthase-enriched ER subdomains publication-title: EMBO J. doi: 10.15252/embj.201695189 contributor: fullname: Nishimura – volume: 18 start-page: 1382 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib52 article-title: Structural and functional analysis of the GABARAP interaction motif (GIM) publication-title: EMBO Rep. doi: 10.15252/embr.201643587 contributor: fullname: Rogov – volume: 584 start-page: 1379 year: 2010 ident: 10.1016/j.molcel.2019.03.033_bib48 article-title: Atg8-family interacting motif crucial for selective autophagy publication-title: FEBS Lett. doi: 10.1016/j.febslet.2010.01.018 contributor: fullname: Noda – volume: 532 start-page: 45 year: 2002 ident: 10.1016/j.molcel.2019.03.033_bib53 article-title: Lymphotoxin-beta receptor mediates NEMO-independent NF-kappaB activation publication-title: FEBS Lett. doi: 10.1016/S0014-5793(02)03622-0 contributor: fullname: Saitoh – volume: 19 start-page: 349 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib6 article-title: Mechanism and medical implications of mammalian autophagy publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/s41580-018-0003-4 contributor: fullname: Dikic – volume: 6 start-page: 301 year: 2010 ident: 10.1016/j.molcel.2019.03.033_bib18 article-title: Electron tomography reveals the endoplasmic reticulum as a membrane source for autophagosome formation publication-title: Autophagy doi: 10.4161/auto.6.2.11134 contributor: fullname: Hayashi-Nishino – volume: 17 start-page: 69 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib50 article-title: Structure and function of ER membrane contact sites with other organelles publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm.2015.8 contributor: fullname: Phillips – volume: 473 start-page: 337 year: 2011 ident: 10.1016/j.molcel.2019.03.033_bib55 article-title: Global quantification of mammalian gene expression control publication-title: Nature doi: 10.1038/nature10098 contributor: fullname: Schwanhäusser – volume: 33 start-page: 1 year: 2008 ident: 10.1016/j.molcel.2019.03.033_bib23 article-title: GFP-like proteins stably accumulate in lysosomes publication-title: Cell Struct. Funct. doi: 10.1247/csf.07011 contributor: fullname: Katayama – volume: 6 start-page: e25555 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib15 article-title: Full length RTN3 regulates turnover of tubular endoplasmic reticulum via selective autophagy publication-title: eLife doi: 10.7554/eLife.25555 contributor: fullname: Grumati – volume: 217 start-page: 3354 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib37 article-title: Atlastins remodel the endoplasmic reticulum for selective autophagy publication-title: J. Cell Biol. doi: 10.1083/jcb.201804185 contributor: fullname: Liang – volume: 85 start-page: 257 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib51 article-title: The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson’s disease publication-title: Neuron doi: 10.1016/j.neuron.2014.12.007 contributor: fullname: Pickrell – volume: 46 start-page: 699 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib39 article-title: Eat it right: ER-phagy and recovER-phagy publication-title: Biochem. Soc. Trans. doi: 10.1042/BST20170354 contributor: fullname: Loi – volume: 74 start-page: 4725 year: 2002 ident: 10.1016/j.molcel.2019.03.033_bib45 article-title: A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics publication-title: Anal. Chem. doi: 10.1021/ac020018n contributor: fullname: Natsume – volume: 53 start-page: 1018 year: 2014 ident: 10.1016/j.molcel.2019.03.033_bib14 article-title: Comprehensive exploration of novel chimeric transcripts in clear cell renal cell carcinomas using whole transcriptome analysis publication-title: Genes Chromosomes Cancer doi: 10.1002/gcc.22211 contributor: fullname: Gotoh – volume: 3 start-page: 452 year: 2007 ident: 10.1016/j.molcel.2019.03.033_bib27 article-title: Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3 publication-title: Autophagy doi: 10.4161/auto.4451 contributor: fullname: Kimura – volume: 522 start-page: 359 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib42 article-title: Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus publication-title: Nature doi: 10.1038/nature14506 contributor: fullname: Mochida – volume: 12 start-page: 982 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib43 article-title: CRISPRscan: designing highly efficient sgRNAs for CRISPR-Cas9 targeting in vivo publication-title: Nat. Methods doi: 10.1038/nmeth.3543 contributor: fullname: Moreno-Mateos – volume: 3 start-page: 655 year: 2007 ident: 10.1016/j.molcel.2019.03.033_bib31 article-title: Sequestration revisited: integrating traditional electron microscopy, de novo assembly and new results publication-title: Autophagy doi: 10.4161/auto.4590 contributor: fullname: Kovács – volume: 18 start-page: E1865 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib67 article-title: Monitoring and measuring autophagy publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms18091865 contributor: fullname: Yoshii – volume: 175 start-page: 121 year: 2006 ident: 10.1016/j.molcel.2019.03.033_bib11 article-title: Role of FIP200 in cardiac and liver development and its regulation of TNFalpha and TSC-mTOR signaling pathways publication-title: J. Cell Biol. doi: 10.1083/jcb.200604129 contributor: fullname: Gan – volume: 26 start-page: 6 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib26 article-title: Ubiquitin-dependent and independent signals in selective autophagy publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2015.08.010 contributor: fullname: Khaminets – volume: 285 start-page: 3499 year: 2010 ident: 10.1016/j.molcel.2019.03.033_bib36 article-title: Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.072389 contributor: fullname: Liang – volume: 282 start-page: 1182 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib64 article-title: Functional roles of transiently and intrinsically disordered regions within proteins publication-title: FEBS J. doi: 10.1111/febs.13202 contributor: fullname: Uversky – volume: 9 start-page: 676 year: 2012 ident: 10.1016/j.molcel.2019.03.033_bib54 article-title: Fiji: an open-source platform for biological-image analysis publication-title: Nat. Methods doi: 10.1038/nmeth.2019 contributor: fullname: Schindelin – volume: 13 start-page: 1211 year: 2008 ident: 10.1016/j.molcel.2019.03.033_bib47 article-title: Structural basis of target recognition by Atg8/LC3 during selective autophagy publication-title: Genes Cells doi: 10.1111/j.1365-2443.2008.01238.x contributor: fullname: Noda – volume: 43 start-page: 2141 year: 2004 ident: 10.1016/j.molcel.2019.03.033_bib69 article-title: Polymer models of protein stability, folding, and interactions publication-title: Biochemistry doi: 10.1021/bi036269n contributor: fullname: Zhou – volume: 39 start-page: 116 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib68 article-title: Systemic analysis of Atg5-null mice rescued from neonatal lethality by transgenic ATG5 expression in neurons publication-title: Dev. Cell doi: 10.1016/j.devcel.2016.09.001 contributor: fullname: Yoshii – volume: 64 start-page: 835 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib22 article-title: An autophagic flux probe that releases an internal control publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.09.037 contributor: fullname: Kaizuka – volume: 217 start-page: 3817 year: 2018 ident: 10.1016/j.molcel.2019.03.033_bib44 article-title: Genome-wide CRISPR screen identifies TMEM41B as a gene required for autophagosome formation publication-title: J. Cell Biol. doi: 10.1083/jcb.201804132 contributor: fullname: Morita – volume: 74 start-page: 3205 year: 2017 ident: 10.1016/j.molcel.2019.03.033_bib30 article-title: Functions of intrinsic disorder in transmembrane proteins publication-title: Cell. Mol. Life Sci. doi: 10.1007/s00018-017-2562-5 contributor: fullname: Kjaergaard – volume: 354 start-page: 1036 year: 2016 ident: 10.1016/j.molcel.2019.03.033_bib63 article-title: The ATG conjugation systems are important for degradation of the inner autophagosomal membrane publication-title: Science doi: 10.1126/science.aaf6136 contributor: fullname: Tsuboyama – volume: 181 start-page: 497 year: 2008 ident: 10.1016/j.molcel.2019.03.033_bib17 article-title: FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells publication-title: J. Cell Biol. doi: 10.1083/jcb.200712064 contributor: fullname: Hara – volume: 14 start-page: 1127 year: 2013 ident: 10.1016/j.molcel.2019.03.033_bib1 article-title: Loss of iron triggers PINK1/Parkin-independent mitophagy publication-title: EMBO Rep. doi: 10.1038/embor.2013.168 contributor: fullname: Allen – volume: 522 start-page: 354 year: 2015 ident: 10.1016/j.molcel.2019.03.033_bib25 article-title: Regulation of endoplasmic reticulum turnover by selective autophagy publication-title: Nature doi: 10.1038/nature14498 contributor: fullname: Khaminets |
SSID | ssj0014589 |
Score | 2.6768816 |
Snippet | Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions... |
SourceID | proquest crossref pubmed elsevier |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 909 |
SubjectTerms | Amino Acid Sequence - genetics Autophagy - genetics Autophagy-Related Proteins - chemistry Autophagy-Related Proteins - genetics Cell Cycle Proteins - genetics Endoplasmic Reticulum - chemistry Endoplasmic Reticulum - genetics Endoplasmic Reticulum Stress - genetics ER-phagy Humans Intracellular Signaling Peptides and Proteins Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - genetics intrinsically disordered region Membrane Proteins Microtubule-Associated Proteins - genetics Neoplasm Proteins - genetics organellar contact site Proteolysis selective autophagy |
Title | Intrinsically Disordered Protein TEX264 Mediates ER-phagy |
URI | https://dx.doi.org/10.1016/j.molcel.2019.03.033 https://www.ncbi.nlm.nih.gov/pubmed/31006538 https://search.proquest.com/docview/2212716432 |
Volume | 74 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3dS8MwED_mhuCL-O38ooKvYWnTj_VRZaJORXTTvYWkSbWi3dD6sP_eu34IPoggFEpCQsMlvfsdd_kdwFGUGCO4NiztxyFDeyxYrCP0UlSqw1hp5QV0wfn6Jjwf-5eTYNKC0-YuDKVV1rq_0umltq57erU0e7Ms691T7NSLQoIgnGDzAnSwyb02dI5PHoZX38EEPygr4dF4RhOaG3Rlmtfb9DWxFINwK7ZTIX6zUL8h0NISna3Acg0hneNqlavQsvkaLFZFJefrEF_kxXuWl9J_nTsNvaY1zi1xMmS5MxpMEKA412WVDvvhDO7Y7Fk9zTdgfDYYnZ6zukACS_zIL5hSHo_C1Dex4dbqoJ-YBCFFoi2iIhd3Bw20i1oER3Hf-joVARfGSzR3tSEssgntfJrbbXBipXziSvf66O-5Cn9r16D_atF9JP6ZtAusEYqcVTwYskkQe5GVECUJUXKBj-hC1EhO_thPiar6j5mHjaAlHnWKX6jcTj8_pEds9OjeCa8LW9UOfK-F4hQhKu-df393F5aoVaaBhXvQLt4_7T4CjkIf1AeK3sO7x-EBLFxMTr4Av4rTUw |
link.rule.ids | 315,786,790,3525,27602,27957,27958,45698,45909 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LS8NAEB6qInoR39ZnBK9LN9lN0hxVKq1aEa3Q27Kb3WhF06L10H_vTB4FDyIIOSUbsny7mfmGmf0G4CxOrRXcWJa1k4ihPxYsMTFGKTozUaKNDkI64Ny_i7pP8noYDhtwWZ-FobLKyvaXNr2w1tWdVoVmazIatR4pdxrEEVEQTrR5AZZkmHDa2r3hxTyVIMOiDx6NZjS8Pj9XFHm9j99SRxkIv9Q6FeI3__Qb_yz80NU6rFUE0jsv57gBDZdvwnLZUnK2BUkvn36M8gL7t5lXi2s6692TIsMo9wadIdITr1_06HCfXueBTV7082wbnq46g8suq9ojsFTGcsq0DngcZdImljtnwnZqUyQUqXHIiXxcG3TPPtoQHMWlkyYTIRc2SA33jSUmsgOL-Th3e-AlWktSSg_aGO35Gn9q32L06jB4JPWZrAmsBkVNShUMVZeHvaoSREUgKi7wEk2Ia-TUj9VUaKj_ePO0BlrhRqfshc7d-OtTBaRFj8GdCJqwW67AfC6UpYjQdO__-7snsNId9G_Vbe_u5gBW6UlREBYdwuL048sdIfWYmuNia30D_-nSgg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Intrinsically+Disordered+Protein+TEX264+Mediates+ER-phagy&rft.jtitle=Molecular+cell&rft.au=Chino%2C+Haruka&rft.au=Hatta%2C+Tomohisa&rft.au=Natsume%2C+Tohru&rft.au=Mizushima%2C+Noboru&rft.date=2019-06-06&rft.eissn=1097-4164&rft.volume=74&rft.issue=5&rft.spage=909&rft_id=info:doi/10.1016%2Fj.molcel.2019.03.033&rft_id=info%3Apmid%2F31006538&rft.externalDocID=31006538 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1097-2765&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1097-2765&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1097-2765&client=summon |