The Hsp70 and TRiC/CCT Chaperone Systems Cooperate In Vivo To Assemble the Von Hippel-Lindau Tumor Suppressor Complex

Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from...

Full description

Saved in:
Bibliographic Details
Published inMolecular and Cellular Biology Vol. 23; no. 9; pp. 3141 - 3151
Main Authors Melville, Mark W., McClellan, Amie J., Meyer, Anne S., Darveau, Andre, Frydman, Judith
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.05.2003
Taylor & Francis
Subjects
Adenosine Triphosphatases
Cell and Organelle Structure and Assembly
Chaperonin Containing TCP-1
Chaperonins - genetics
Chaperonins - metabolism
Cytosol - metabolism
Elongin
Fungal Proteins - genetics
Fungal Proteins - metabolism
Genes, Tumor Suppressor
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Humans
Intracellular Signaling Peptides and Proteins
Ligases - genetics
Ligases - metabolism
Macromolecular Substances
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Molecular Chaperones - metabolism
Mutation
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Protein Folding
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
t-Complex Genome Region
Temperature
Transcription Factors - genetics
Transcription Factors - metabolism
Tumor Suppressor Proteins
Ubiquitin-Protein Ligases
Von Hippel-Lindau Tumor Suppressor Protein
Online AccessGet full text
ISSN0270-7306
1098-5549
1098-5549
DOI10.1128/MCB.23.9.3141-3151.2003

Cover

Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList The degree of cooperation and redundancy between different chaperones is an important problem in understanding how proteins fold in the cell. Here we use the yeast Saccharomyces cerevisiae as a model system to examine in vivo the chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor suppressor complex. VHL and elongin BC expressed in yeast assembled into a correctly folded VBC complex that resembles the complex from mammalian cells. Unassembled VHL did not fold and remained associated with the cytosolic chaperones Hsp70 and TRiC/CCT, in agreement with results from mammalian cells. Analysis of the folding reaction in yeast strains carrying conditional chaperone mutants indicates that incorporation of VHL into VBC requires both functional TRiC and Hsp70. VBC assembly was defective in cells carrying either a temperature-sensitive ssa1 gene as their sole source of cytosolic Hsp70/SSA function or a temperature-sensitive mutation in CCT4, a subunit of the TRiC/CCT complex. Analysis of the VHL-chaperone interactions in these strains revealed that the cct4ts mutation decreased binding to TRiC but did not affect the interaction with Hsp70. In contrast, loss of Hsp70 function disrupted the interaction of VHL with both Hsp70 and TRiC. We conclude that, in vivo, folding of some polypeptides requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC.
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
The degree of cooperation and redundancy between different chaperones is an important problem in understanding how proteins fold in the cell. Here we use the yeast Saccharomyces cerevisiae as a model system to examine in vivo the chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor suppressor complex. VHL and elongin BC expressed in yeast assembled into a correctly folded VBC complex that resembles the complex from mammalian cells. Unassembled VHL did not fold and remained associated with the cytosolic chaperones Hsp70 and TRiC/CCT, in agreement with results from mammalian cells. Analysis of the folding reaction in yeast strains carrying conditional chaperone mutants indicates that incorporation of VHL into VBC requires both functional TRiC and Hsp70. VBC assembly was defective in cells carrying either a temperature-sensitive ssa1 gene as their sole source of cytosolic Hsp70/SSA function or a temperature-sensitive mutation in CCT4, a subunit of the TRiC/CCT complex. Analysis of the VHL-chaperone interactions in these strains revealed that the cct4ts mutation decreased binding to TRiC but did not affect the interaction with Hsp70. In contrast, loss of Hsp70 function disrupted the interaction of VHL with both Hsp70 and TRiC. We conclude that, in vivo, folding of some polypeptides requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC.The degree of cooperation and redundancy between different chaperones is an important problem in understanding how proteins fold in the cell. Here we use the yeast Saccharomyces cerevisiae as a model system to examine in vivo the chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor suppressor complex. VHL and elongin BC expressed in yeast assembled into a correctly folded VBC complex that resembles the complex from mammalian cells. Unassembled VHL did not fold and remained associated with the cytosolic chaperones Hsp70 and TRiC/CCT, in agreement with results from mammalian cells. Analysis of the folding reaction in yeast strains carrying conditional chaperone mutants indicates that incorporation of VHL into VBC requires both functional TRiC and Hsp70. VBC assembly was defective in cells carrying either a temperature-sensitive ssa1 gene as their sole source of cytosolic Hsp70/SSA function or a temperature-sensitive mutation in CCT4, a subunit of the TRiC/CCT complex. Analysis of the VHL-chaperone interactions in these strains revealed that the cct4ts mutation decreased binding to TRiC but did not affect the interaction with Hsp70. In contrast, loss of Hsp70 function disrupted the interaction of VHL with both Hsp70 and TRiC. We conclude that, in vivo, folding of some polypeptides requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC.
The degree of cooperation and redundancy between different chaperones is an important problem in understanding how proteins fold in the cell. Here we use the yeast Saccharomyces cerevisiae as a model system to examine in vivo the chaperone requirements for assembly of the von Hippel-Lindau protein (VHL)-elongin BC (VBC) tumor suppressor complex. VHL and elongin BC expressed in yeast assembled into a correctly folded VBC complex that resembles the complex from mammalian cells. Unassembled VHL did not fold and remained associated with the cytosolic chaperones Hsp70 and TRiC/CCT, in agreement with results from mammalian cells. Analysis of the folding reaction in yeast strains carrying conditional chaperone mutants indicates that incorporation of VHL into VBC requires both functional TRiC and Hsp70. VBC assembly was defective in cells carrying either a temperature-sensitive ssa1 gene as their sole source of cytosolic Hsp70/SSA function or a temperature-sensitive mutation in CCT4 , a subunit of the TRiC/CCT complex. Analysis of the VHL-chaperone interactions in these strains revealed that the cct4ts mutation decreased binding to TRiC but did not affect the interaction with Hsp70. In contrast, loss of Hsp70 function disrupted the interaction of VHL with both Hsp70 and TRiC. We conclude that, in vivo, folding of some polypeptides requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC.
Author Judith Frydman
Amie J. McClellan
Anne S. Meyer
Andre Darveau
Mark W. Melville
AuthorAffiliation Department of Biological Sciences, Stanford University, Stanford, California 94305, 1 Departement de Biochimie et Microbiologie, CREFSIP, Université Laval, Sainte-Foy, Quebec, Canada 2
AuthorAffiliation_xml – name: Department of Biological Sciences, Stanford University, Stanford, California 94305, 1 Departement de Biochimie et Microbiologie, CREFSIP, Université Laval, Sainte-Foy, Quebec, Canada 2
Author_xml – sequence: 1
  givenname: Mark W.
  surname: Melville
  fullname: Melville, Mark W.
  organization: Department of Biological Sciences, Stanford University
– sequence: 2
  givenname: Amie J.
  surname: McClellan
  fullname: McClellan, Amie J.
  organization: Department of Biological Sciences, Stanford University
– sequence: 3
  givenname: Anne S.
  surname: Meyer
  fullname: Meyer, Anne S.
  organization: Department of Biological Sciences, Stanford University
– sequence: 4
  givenname: Andre
  surname: Darveau
  fullname: Darveau, Andre
  organization: Departement de Biochimie et Microbiologie, CREFSIP, Université Laval, Sainte-Foy
– sequence: 5
  givenname: Judith
  surname: Frydman
  fullname: Frydman, Judith
  email: jfrydman@stanford.edu
  organization: Department of Biological Sciences, Stanford University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/12697815$$D View this record in MEDLINE/PubMed
BookMark eNqFkktv1DAUhS1URB_wF8BsusvUj8SOFyzaCJhKg5Bo6NbyZG46Rokd7KRl_j2OprTAZla2fL9z7pF8TtGR8w4QekfJglJWXnyprhaML9SC05xmnBZ0wQjhL9AJJarMiiJXR-iEMEkyyYk4Rqcx_iCECEX4K3RMmVCypMUJmuot4GUcJMHGbXD9zVYXVVXjamsGCGkpvtnFEfqIK-_TixkBXzt8a-89rj2-jBH6dQd4TDa33uGlHQbospV1GzPheup9wDfTMASIMV0r3w8d_HqNXrami_Dm8TxD3z99rKtltvr6-bq6XGVNLtWYrVsObSkEhwZASWGKkhsulaAiB9kQUTC-EbBpoJFFWRZGKlUKJoCwnDJl-Bn6sPcdpnU_c24MptNDsL0JO-2N1f9OnN3qO3-vacGpypP-_FEf_M8J4qh7GxvoOuPAT1HLRFFWHAZpmVBGRALf_p3oKcqfH3mO3AQfY4BWN3Y0o_VzQNtpSvTcAJ0aoBnXSs8N0HMD9NyApJf_6Z9WHFRe7ZXWtT705sGHbqNHs-t8aINxjY2JPmjyfm-ytXfbBxtAm9jrvlk_0_w3sfrVHA
CitedBy_id crossref_primary_10_1016_j_jmb_2010_06_050
crossref_primary_10_1002_bip_21426
crossref_primary_10_1074_jbc_M311225200
crossref_primary_10_3389_fonc_2022_961733
crossref_primary_10_1371_journal_pgen_1009183
crossref_primary_10_1016_j_mocell_2024_100012
crossref_primary_10_1016_j_bpj_2016_04_045
crossref_primary_10_1016_j_febslet_2004_06_040
crossref_primary_10_1016_j_molcel_2013_01_020
crossref_primary_10_1073_pnas_2018127118
crossref_primary_10_1002_pro_531
crossref_primary_10_3390_ijms161125975
crossref_primary_10_1016_j_bbrc_2017_05_020
crossref_primary_10_1016_j_celrep_2014_09_056
crossref_primary_10_1096_fj_12_210146
crossref_primary_10_1016_j_cell_2019_03_012
crossref_primary_10_3390_v11020107
crossref_primary_10_1172_JCI146536
crossref_primary_10_1016_j_febslet_2013_07_019
crossref_primary_10_1186_s12957_020_01911_x
crossref_primary_10_1371_journal_pone_0066333
crossref_primary_10_1074_jbc_M113_460691
crossref_primary_10_1007_s12192_013_0413_3
crossref_primary_10_1128_mbio_00499_24
crossref_primary_10_1038_s41598_018_31726_6
crossref_primary_10_1073_pnas_1108537109
crossref_primary_10_1074_jbc_M803742200
crossref_primary_10_1016_j_biocel_2005_12_019
crossref_primary_10_7554_eLife_31926
crossref_primary_10_1038_ncb0805_736
crossref_primary_10_1091_mbc_E14_08_1262
crossref_primary_10_1371_journal_pone_0060895
crossref_primary_10_1007_s12192_008_0057_x
crossref_primary_10_1016_j_molcel_2006_08_017
crossref_primary_10_1016_j_bbamcr_2021_119187
crossref_primary_10_1515_revneuro_2016_0035
crossref_primary_10_1371_journal_pone_0279851
crossref_primary_10_1016_j_jmb_2021_166958
crossref_primary_10_1016_j_molcel_2018_03_016
crossref_primary_10_1016_j_jprot_2021_104169
crossref_primary_10_1097_MD_0000000000033219
crossref_primary_10_1074_jbc_M900097200
crossref_primary_10_1016_j_cytogfr_2008_08_006
crossref_primary_10_1111_cmi_12719
crossref_primary_10_1111_febs_14322
crossref_primary_10_1016_j_str_2015_04_015
crossref_primary_10_1016_j_molcel_2020_06_003
crossref_primary_10_1111_j_1742_4658_2007_06075_x
crossref_primary_10_1128_MCB_24_18_8069_8079_2004
crossref_primary_10_1007_s12192_018_0949_3
crossref_primary_10_1016_j_febslet_2004_11_034
crossref_primary_10_1038_s41598_021_91086_6
crossref_primary_10_1016_j_tins_2008_07_004
crossref_primary_10_1016_j_molcel_2013_05_002
crossref_primary_10_4061_2011_843206
crossref_primary_10_1016_j_canlet_2024_216844
crossref_primary_10_1038_s41598_018_32009_w
crossref_primary_10_1016_j_cell_2005_11_039
crossref_primary_10_1016_j_jmb_2008_01_011
crossref_primary_10_1146_annurev_biophys_051013_022653
crossref_primary_10_1016_j_molmed_2004_02_004
crossref_primary_10_1155_2019_1687340
crossref_primary_10_1038_nsmb_1515
crossref_primary_10_1016_j_molcel_2006_09_003
crossref_primary_10_1016_j_tcb_2004_09_015
crossref_primary_10_1038_ncb1477
crossref_primary_10_1128_JVI_03186_12
crossref_primary_10_1038_nm_2056
crossref_primary_10_1016_j_cell_2005_03_024
crossref_primary_10_1074_jbc_M503615200
crossref_primary_10_1007_s00438_022_01940_z
crossref_primary_10_1016_j_bcmd_2011_11_004
crossref_primary_10_1074_jbc_M115_684878
crossref_primary_10_1128_MMBR_05018_11
crossref_primary_10_1242_jcs_184846
crossref_primary_10_1074_jbc_REV118_002810
crossref_primary_10_1016_j_cstres_2024_01_003
crossref_primary_10_1158_1541_7786_MCR_12_0117
crossref_primary_10_1038_nature07195
crossref_primary_10_1002_pmic_200300916
crossref_primary_10_1371_journal_pone_0052099
crossref_primary_10_3390_ijms24054710
crossref_primary_10_1038_sj_emboj_7600854
crossref_primary_10_1080_13816810_2022_2138455
crossref_primary_10_1091_mbc_E16_04_0224
crossref_primary_10_18632_oncotarget_28653
crossref_primary_10_1111_j_1567_1364_2008_00425_x
crossref_primary_10_1136_jmg_2023_109550
crossref_primary_10_1016_S1097_2765_03_00423_4
crossref_primary_10_1038_s41564_025_01947_3
crossref_primary_10_1016_j_ijbiomac_2020_10_134
crossref_primary_10_1038_nrm1492
crossref_primary_10_1126_sciadv_ade1207
crossref_primary_10_1016_j_freeradbiomed_2021_01_016
crossref_primary_10_1016_j_jmb_2021_167399
crossref_primary_10_1016_j_celrep_2012_12_007
crossref_primary_10_1016_j_canlet_2015_12_029
crossref_primary_10_1038_nsmb_1464
crossref_primary_10_1038_cddis_2017_425
crossref_primary_10_1007_s12192_021_01237_x
crossref_primary_10_1002_jcb_25669
crossref_primary_10_1038_labinvest_3700684
crossref_primary_10_1074_mcp_M114_044560
crossref_primary_10_1002_mrd_22925
Cites_doi 10.1126/science.284.5414.657
10.1006/excr.2000.5139
10.1016/S0092-8674(00)80787-4
10.1128/MCB.22.6.1947-1960.2002
10.1126/science.1068408
10.1006/bbrc.1997.7819
10.1073/pnas.96.17.9533
10.1038/415141a
10.1126/science.272.5267.1497
10.1038/370373a0
10.1016/S0968-0004(97)01005-0
10.1007/BF00175490
10.1002/j.1460-2075.1991.tb04891.x
10.1038/20459
10.1146/annurev.biochem.70.1.603
10.1073/pnas.91.19.9116
10.1073/pnas.96.22.12436
10.1016/S0092-8674(00)80806-5
10.1038/370111a0
10.1038/415180a
10.1023/A:1005663728291
10.1101/gad.13.14.1822
10.1073/pnas.94.6.2156
10.1093/emboj/18.1.75
10.1016/S0076-6879(99)06010-3
10.1016/S0167-4781(00)00052-X
10.1002/(SICI)1097-0061(199605)12:6<523::AID-YEA962>3.0.CO;2-C
10.1016/S0092-8674(00)80928-9
10.1016/0022-1759(89)90210-X
10.1126/science.1059817
10.1016/S1097-2765(00)80233-6
10.1006/jsbi.2001.4380
10.1126/science.1059796
10.1128/MCB.16.8.4378
10.1093/emboj/18.1.85
10.1038/23301
10.1073/pnas.97.15.8507
10.1016/S0065-230X(01)82003-0
10.1126/science.7939687
10.1515/bchm.1998.379.3.301
10.1016/S0092-8674(00)81446-4
10.1006/jmbi.2001.4938
10.1016/S0968-0004(99)01445-0
10.1073/pnas.95.22.12860
10.1038/35017054
ContentType Journal Article
Copyright Copyright © 2003, American Society for Microbiology 2003
Copyright_xml – notice: Copyright © 2003, American Society for Microbiology 2003
DBID AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
7TO
8FD
FR3
H94
P64
RC3
7X8
5PM
DOI 10.1128/MCB.23.9.3141-3151.2003
DatabaseName CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
Oncogenes and Growth Factors Abstracts
Technology Research Database
Engineering Research Database
AIDS and Cancer Research Abstracts
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
AIDS and Cancer Research Abstracts
Genetics Abstracts
Engineering Research Database
Oncogenes and Growth Factors Abstracts
Technology Research Database
Biotechnology and BioEngineering Abstracts
MEDLINE - Academic
DatabaseTitleList
AIDS and Cancer Research Abstracts

MEDLINE - Academic

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 Chemistry
Biology
EISSN 1098-5549
EndPage 3151
ExternalDocumentID PMC153194
12697815
10_1128_MCB_23_9_3141_3151_2003
12267305
mcb_23_9_3141
Genre Research Article
Research Support, U.S. Gov't, Non-P.H.S
Research Support, U.S. Gov't, P.H.S
Research Support, Non-U.S. Gov't
Journal Article
GrantInformation_xml – fundername: NIGMS NIH HHS
  grantid: R01 GM056433
– fundername: NIGMS NIH HHS
  grantid: F32 GM064992
– fundername: NCI NIH HHS
  grantid: T32 CA009302
– fundername: NCI NIH HHS
  grantid: CA09302
– fundername: NIGMS NIH HHS
  grantid: GM64992
– fundername: NIGMS NIH HHS
  grantid: R37 GM056433
– fundername: NIGMS NIH HHS
  grantid: GM56433
GroupedDBID ---
-DZ
-~X
.55
.GJ
0R~
123
18M
29M
2WC
39C
3O-
4.4
53G
5RE
5VS
9M8
ACGFO
ACKIV
ACNCT
ADBBV
ADIYS
AENEX
AEOZL
AFFNX
AGHSJ
AGVNZ
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BTFSW
C1A
CS3
DIK
DU5
E3Z
EBS
EJD
F5P
GX1
H13
HH5
HYE
HZ~
IH2
KQ8
L7B
M4Z
MVM
N9A
O9-
OK1
P2P
RHF
RHI
RNS
RPM
RSF
TDBHL
TFL
TFW
TR2
UCJ
UDS
VQA
W8F
WH7
WHG
WOQ
X7M
Y6R
ZCA
ZGI
AAGFI
AAYXX
ABJNI
ADXHL
AMPGV
CITATION
ABRLO
ABTAH
CGR
CUY
CVF
ECM
EIF
EMOBN
NPM
PKN
YIN
YYP
ZXP
ZY4
7TO
8FD
FR3
H94
P64
RC3
TASJS
7X8
5PM
ID FETCH-LOGICAL-c479t-bf3ef8663ecee976a583a3796164e7c06523d6edcec75885a7998626e024129a3
ISSN 0270-7306
1098-5549
IngestDate Thu Aug 21 13:59:14 EDT 2025
Fri Sep 05 00:01:15 EDT 2025
Thu Sep 04 18:16:53 EDT 2025
Wed Feb 19 02:34:14 EST 2025
Tue Jul 01 01:05:41 EDT 2025
Thu Apr 24 23:10:03 EDT 2025
Wed Dec 25 09:06:07 EST 2024
Wed May 18 15:25:55 EDT 2016
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 9
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c479t-bf3ef8663ecee976a583a3796164e7c06523d6edcec75885a7998626e024129a3
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
Corresponding author. Mailing address: Department of Biological Sciences, Stanford University, Stanford, CA 94305. Phone: (650) 725-7833. Fax: (650) 723-8475. E-mail: jfrydman@stanford.edu.
Present address: Wyeth BioPharma, Andover, MA 01810.
PMID 12697815
PQID 18731206
PQPubID 23462
PageCount 11
ParticipantIDs pubmed_primary_12697815
crossref_citationtrail_10_1128_MCB_23_9_3141_3151_2003
crossref_primary_10_1128_MCB_23_9_3141_3151_2003
proquest_miscellaneous_73191254
informaworld_taylorfrancis_310_1128_MCB_23_9_3141_3151_2003
highwire_asm_mcb_23_9_3141
pubmedcentral_primary_oai_pubmedcentral_nih_gov_153194
proquest_miscellaneous_18731206
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 20030501
5/1/2003
2003-05-01
2003-May
PublicationDateYYYYMMDD 2003-05-01
PublicationDate_xml – month: 05
  year: 2003
  text: 20030501
  day: 01
PublicationDecade 2000
PublicationPlace United States
PublicationPlace_xml – name: United States
PublicationTitle Molecular and Cellular Biology
PublicationTitleAlternate Mol Cell Biol
PublicationYear 2003
Publisher American Society for Microbiology
Taylor & Francis
Publisher_xml – name: American Society for Microbiology
– name: Taylor & Francis
References Heyrovska N. (R23) 1998; 379
R41
R40
R21
R43
R20
R42
R45
R22
R44
R25
R47
R24
R46
R27
R26
R28
Botuyan M. V. (R6) 2001; 312
R1
R2
Manning K. U. (R35) 1991; 10
R4
R5
R7
R8
R9
Gregersen N. (R19) 2000; 23
R30
James P. (R29) 1995; 6
R10
R32
R31
R12
R34
R11
R33
Bazin R. (R3) 1989; 116
R14
R36
R13
R16
R38
R15
R37
R18
R17
R39
References_xml – ident: R30
  doi: 10.1126/science.284.5414.657
– ident: R32
  doi: 10.1006/excr.2000.5139
– ident: R44
  doi: 10.1016/S0092-8674(00)80787-4
– ident: R21
  doi: 10.1128/MCB.22.6.1947-1960.2002
– ident: R22
  doi: 10.1126/science.1068408
– ident: R1
  doi: 10.1006/bbrc.1997.7819
– ident: R40
  doi: 10.1073/pnas.96.17.9533
– ident: R18
  doi: 10.1038/415141a
– ident: R15
  doi: 10.1126/science.272.5267.1497
– ident: R37
  doi: 10.1038/370373a0
– ident: R16
  doi: 10.1016/S0968-0004(97)01005-0
– ident: R5
  doi: 10.1007/BF00175490
– volume: 10
  start-page: 3273
  year: 1991
  ident: R35
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1991.tb04891.x
– ident: R36
  doi: 10.1038/20459
– ident: R14
  doi: 10.1146/annurev.biochem.70.1.603
– ident: R47
  doi: 10.1073/pnas.91.19.9116
– ident: R26
  doi: 10.1073/pnas.96.22.12436
– ident: R7
  doi: 10.1016/S0092-8674(00)80806-5
– ident: R17
  doi: 10.1038/370111a0
– ident: R24
  doi: 10.1038/415180a
– volume: 23
  start-page: 441
  year: 2000
  ident: R19
  publication-title: J. Inherit. Metab. Dis.
  doi: 10.1023/A:1005663728291
– ident: R34
  doi: 10.1101/gad.13.14.1822
– ident: R39
  doi: 10.1073/pnas.94.6.2156
– ident: R42
  doi: 10.1093/emboj/18.1.75
– ident: R33
  doi: 10.1016/S0076-6879(99)06010-3
– ident: R28
  doi: 10.1016/S0167-4781(00)00052-X
– volume: 6
  start-page: 33
  year: 1995
  ident: R29
  publication-title: Mol. Biol. Cell
– ident: R43
  doi: 10.1002/(SICI)1097-0061(199605)12:6<523::AID-YEA962>3.0.CO;2-C
– ident: R8
  doi: 10.1016/S0092-8674(00)80928-9
– volume: 116
  start-page: 245
  year: 1989
  ident: R3
  publication-title: J. Immunol. Methods
  doi: 10.1016/0022-1759(89)90210-X
– ident: R25
  doi: 10.1126/science.1059817
– ident: R13
  doi: 10.1016/S1097-2765(00)80233-6
– ident: R12
  doi: 10.1006/jsbi.2001.4380
– ident: R27
  doi: 10.1126/science.1059796
– ident: R4
  doi: 10.1128/MCB.16.8.4378
– ident: R45
  doi: 10.1093/emboj/18.1.85
– ident: R10
  doi: 10.1038/23301
– ident: R41
  doi: 10.1073/pnas.97.15.8507
– ident: R9
  doi: 10.1016/S0065-230X(01)82003-0
– ident: R20
  doi: 10.1126/science.7939687
– volume: 379
  start-page: 301
  year: 1998
  ident: R23
  publication-title: Biol. Chem.
  doi: 10.1515/bchm.1998.379.3.301
– ident: R46
  doi: 10.1016/S0092-8674(00)81446-4
– ident: R2
– volume: 312
  start-page: 177
  year: 2001
  ident: R6
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.2001.4938
– ident: R11
  doi: 10.1016/S0968-0004(99)01445-0
– ident: R31
  doi: 10.1073/pnas.95.22.12860
– ident: R38
  doi: 10.1038/35017054
SSID ssj0006903
Score 2.110521
Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
The degree of cooperation and redundancy between different chaperones is an important problem in understanding how proteins fold in the cell. Here we use the...
SourceID pubmedcentral
proquest
pubmed
crossref
informaworld
highwire
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 3141
SubjectTerms Adenosine Triphosphatases
Cell and Organelle Structure and Assembly
Chaperonin Containing TCP-1
Chaperonins - genetics
Chaperonins - metabolism
Cytosol - metabolism
Elongin
Fungal Proteins - genetics
Fungal Proteins - metabolism
Genes, Tumor Suppressor
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Humans
Intracellular Signaling Peptides and Proteins
Ligases - genetics
Ligases - metabolism
Macromolecular Substances
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Molecular Chaperones - metabolism
Mutation
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Protein Folding
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
t-Complex Genome Region
Temperature
Transcription Factors - genetics
Transcription Factors - metabolism
Tumor Suppressor Proteins
Ubiquitin-Protein Ligases
Von Hippel-Lindau Tumor Suppressor Protein
Title The Hsp70 and TRiC/CCT Chaperone Systems Cooperate In Vivo To Assemble the Von Hippel-Lindau Tumor Suppressor Complex
URI http://mcb.asm.org/content/23/9/3141.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.23.9.3141-3151.2003
https://www.ncbi.nlm.nih.gov/pubmed/12697815
https://www.proquest.com/docview/18731206
https://www.proquest.com/docview/73191254
https://pubmed.ncbi.nlm.nih.gov/PMC153194
Volume 23
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9NAEF5BEYILgvJKee2BW-Q0fq5XnMC0iqApAiVSbyt7s1YtObGV2BHl1zOzfqa0CnCJnHgdP-bz7je7M98Q8p77C-bIODK8kHNwUGxpRBgmFseW40YOj7iF-c7Tc28yd75cuBfdnK7OLimikfx1Y17J_1gVfgO7YpbsP1i2_VP4AbbBvvAJFobPv7bxZJOzsV4CmP1IApS7DWaYzosC4EAgK6XmzVBmWY76yVojZJtsMySdQJzVElOnkH1uAQeTJM9VamhHvRwW5TJbDzdlroNlYVPHn6uffUI7bcrrVglyKk31l1rbqTWnSreYdNhkBw3bmZ2pDFIMwKqUDJaJ6tappuqqLrUNY0E3Rfs5XG9VWLbRmDvzFr0owbp7s9jYgP7F6_fFVe5xjTne61hts9LH-rPHtzCLYRp8Gln2iI-wHYwrrnb97W6Qaxb2z7-J0_nZmZidXMzuknsWY3px_-v3TmPe47qednt9dVQgnOj4ltPscppGZ_qa-O1NLsz1SNwetZk9Jo9qn4R-rAD2hNxRq0Nyv6pSenVIHgRNUcCnpATIUQ05CvamCLljABxtAUdrwNEWcDRZUQQcLTLaAI4C4CgAju4AjmrA0Q5wtAbcMzI_PZkFE6Ou3GFIh_HCiGJbxT6QWQUcDAhv6Pp2aDPugXOumATaa9kLD29bgr_quyEDrx9cawWMEQhoaD8nByu45peE-h4MwL6rwC-OnZBHETNZtMDFaUsxU4YD4jXPXsha1h6rq6RCu7eWL8BowrIFF2g0gUbD2qv2gIzbA_NK2WX_IUeNcUW4WYqljLpmA_Khb25R6Bm3uCqPAy32_fW7Bh0CTCr1m6eyciNMn9mmNfZubwH7OfgpzoC8qNDU3Y_loaadCw9pB2dtAxSX392zSi61yLyJg7NztPekr8jD7u1-TQ6KdaneAE8vorf6tfoNcxTmBg
linkProvider Colorado Alliance of Research Libraries
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=The+Hsp70+and+TRiC%2FCCT+chaperone+systems+cooperate+in+vivo+to+assemble+the+von+Hippel-Lindau+tumor+suppressor+complex&rft.jtitle=Molecular+and+cellular+biology&rft.au=Melville%2C+Mark+W&rft.au=McClellan%2C+Amie+J&rft.au=Meyer%2C+Anne+S&rft.au=Darveau%2C+Andre&rft.date=2003-05-01&rft.issn=0270-7306&rft.volume=23&rft.issue=9&rft.spage=3141&rft_id=info:doi/10.1128%2FMCB.23.9.3141-3151.2003&rft.externalDBID=NO_FULL_TEXT
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0270-7306&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0270-7306&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0270-7306&client=summon