Modulation of store-operated calcium entry and nascent adhesion by p21-activated kinase 1
Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomer...
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| Published in | Experimental & molecular medicine Vol. 50; no. 5; pp. 1 - 10 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
21.05.2018
Springer Nature B.V Nature Publishing Group 생화학분자생물학회 |
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| Online Access | Get full text |
| ISSN | 1226-3613 2092-6413 2092-6413 |
| DOI | 10.1038/s12276-018-0093-2 |
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| Abstract | Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions.
Cancer: Mediating metastatic migration
A molecular mechanism underlying cell movement may contribute to the aggressive migration of metastatic tumor cells. A team led by Ki-Duk Song at Chonbuk National University, Jeonju-si, and Joong-Kook Choi at Chungbuk National University, Cheongju in South Korea investigated the function of a protein called p21-activated kinase 1 (PAK1). PAK1 is known to contribute to the reorganization of cellular structure. The researchers determined that it directly interacts with molecular machinery that controls the storage and release of stockpiled calcium ions at the periphery of the cell where migration takes place. These ions play an important role in enabling cell movement and attachment, and the researchers showed that they could disrupt cellular calcium ion accumulation by switching off the gene encoding PAK1. They now aim to investigate how this mechanism contributes to cancer cell migration. |
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| AbstractList | Cancer: Mediating metastatic migration A molecular mechanism underlying cell movement may contribute to the aggressive migration of metastatic tumor cells. A team led by Ki-Duk Song at Chonbuk National University, Jeonju-si, and Joong-Kook Choi at Chungbuk National University, Cheongju in South Korea investigated the function of a protein called p21-activated kinase 1 (PAK1). PAK1 is known to contribute to the reorganization of cellular structure. The researchers determined that it directly interacts with molecular machinery that controls the storage and release of stockpiled calcium ions at the periphery of the cell where migration takes place. These ions play an important role in enabling cell movement and attachment, and the researchers showed that they could disrupt cellular calcium ion accumulation by switching off the gene encoding PAK1. They now aim to investigate how this mechanism contributes to cancer cell migration. Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions.Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions. Calcium mobilization is necessary for cell movement during embryonicdevelopment, lymphocyte synapse formation, wound healing, and cancer cellmetastasis. Depletion of calcium in the lumen of the endoplasmic reticulum usinginositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerizationand cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) tothe plasma membrane, where it interacts with the calcium release-activated calciumchannel Orai1 to mediate calcium influx; this process is referred to asstore-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulationis associated with cancer cell motility and metastasis. The p21-activated kinases(PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletalorganization, protrusive activity, and cell migration. Although cytoskeletalremodeling apparently contributes to calcium mobilization via SOCE, and vice versa,the mechanisms by which they regulate each other remain unclear. In this study, weaimed to characterize whether PAK1 modulates calcium mobilization and STIM1localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and thatthis interaction was enhanced by treatment with a nascent adhesion inducer, such asphorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared toprimarily colocalize in the cytosol, whereas treatment with PDBu induced theircolocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediatedcalcium mobilization via SOCE. Based on these findings, we propose that PAK1interacts with STIM1 to regulate calcium mobilization and the formation of cellularadhesions. Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions. KCI Citation Count: 0 Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions. A molecular mechanism underlying cell movement may contribute to the aggressive migration of metastatic tumor cells. A team led by Ki-Duk Song at Chonbuk National University, Jeonju-si, and Joong-Kook Choi at Chungbuk National University, Cheongju in South Korea investigated the function of a protein called p21-activated kinase 1 (PAK1). PAK1 is known to contribute to the reorganization of cellular structure. The researchers determined that it directly interacts with molecular machinery that controls the storage and release of stockpiled calcium ions at the periphery of the cell where migration takes place. These ions play an important role in enabling cell movement and attachment, and the researchers showed that they could disrupt cellular calcium ion accumulation by switching off the gene encoding PAK1. They now aim to investigate how this mechanism contributes to cancer cell migration. Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions. Cancer: Mediating metastatic migration A molecular mechanism underlying cell movement may contribute to the aggressive migration of metastatic tumor cells. A team led by Ki-Duk Song at Chonbuk National University, Jeonju-si, and Joong-Kook Choi at Chungbuk National University, Cheongju in South Korea investigated the function of a protein called p21-activated kinase 1 (PAK1). PAK1 is known to contribute to the reorganization of cellular structure. The researchers determined that it directly interacts with molecular machinery that controls the storage and release of stockpiled calcium ions at the periphery of the cell where migration takes place. These ions play an important role in enabling cell movement and attachment, and the researchers showed that they could disrupt cellular calcium ion accumulation by switching off the gene encoding PAK1. They now aim to investigate how this mechanism contributes to cancer cell migration. Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis. Depletion of calcium in the lumen of the endoplasmic reticulum using inositol triphosphate (IP3) or thapsigargin (TG) is known to induce oligomerization and cytoskeleton-mediated translocation of stromal interaction molecule 1 (STIM1) to the plasma membrane, where it interacts with the calcium release-activated calcium channel Orai1 to mediate calcium influx; this process is referred to as store-operated calcium entry (SOCE). Furthermore, aberrant STIM1 or SOCE regulation is associated with cancer cell motility and metastasis. The p21-activated kinases (PAKs), which are downstream effectors of GTPases, reportedly regulate cytoskeletal organization, protrusive activity, and cell migration. Although cytoskeletal remodeling apparently contributes to calcium mobilization via SOCE, and vice versa, the mechanisms by which they regulate each other remain unclear. In this study, we aimed to characterize whether PAK1 modulates calcium mobilization and STIM1 localization. Our data demonstrate that PAK1 interacts with STIM1 in vitro and that this interaction was enhanced by treatment with a nascent adhesion inducer, such as phorbol 12,13-dibutyrate (PDBu). Under basal conditions, both proteins appeared to primarily colocalize in the cytosol, whereas treatment with PDBu induced their colocalization to vinculin-positive peripheral adhesions. Downregulation of PAK1 activity via chemical inhibitors or by PAK1 shDNA expression impaired STIM1-mediated calcium mobilization via SOCE. Based on these findings, we propose that PAK1 interacts with STIM1 to regulate calcium mobilization and the formation of cellular adhesions. |
| Author | Shin, Eun-Young Kim, Hye-Ryun Choi, Joong-Kook Kim, Eung-Gook Jeon, In-Sook Song, Ki-Duk Lee, Hak-Kyo Han, Heon-Seok Hong, Jin-Tae |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29780159$$D View this record in MEDLINE/PubMed https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002348013$$DAccess content in National Research Foundation of Korea (NRF) |
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| CitedBy_id | crossref_primary_10_1016_j_jsbmb_2020_105773 crossref_primary_10_1007_s00441_024_03885_8 crossref_primary_10_1007_s13258_022_01230_3 crossref_primary_10_1016_j_mtcomm_2020_101394 crossref_primary_10_1007_s12272_020_01226_1 crossref_primary_10_1016_j_biopha_2020_111126 |
| Cites_doi | 10.1016/j.tcb.2011.01.002 10.1016/S0968-0004(99)01442-5 10.1093/emboj/17.22.6527 10.1016/j.cub.2005.05.055 10.1152/ajpcell.00418.2012 10.1016/S0960-9822(97)70091-5 10.1042/BST0330891 10.1038/onc.2014.366 10.1016/S0955-0674(97)80156-1 10.1091/mbc.e03-08-0604 10.1038/nchembio.619 10.1016/j.ceca.2007.03.002 10.1128/MCB.24.9.3849-3859.2004 10.1113/JP271142 10.1016/j.cub.2007.12.050 10.1038/nature04147 10.1038/ncb0408-384 10.1016/j.bbamcr.2015.05.011 10.1074/jbc.M112.422295 10.1042/BST0330646 10.1016/j.cellsig.2014.12.017 10.1007/s10059-013-2268-7 10.1016/j.cell.2009.04.065 10.1016/S0092-8674(00)81977-7 10.1016/S0960-9822(98)00398-4 10.1042/bj3480241 10.3389/fncel.2015.00153 10.1083/jcb.201010059 10.1182/blood-2008-06-160861 10.1016/j.bbrc.2014.04.064 10.1042/BJ20041638 10.1016/j.cub.2005.06.035 10.1371/journal.pone.0073063 10.1152/ajpheart.00260.2015 10.1002/bies.20558 10.1091/mbc.02-02-0015 10.1152/physrev.00020.2014 10.1016/j.bbamcr.2014.10.027 10.1016/j.bcp.2011.05.017 10.1161/CIRCEP.113.001198 |
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| References | Stofega, Sanders, Gardiner, Bokoch (CR28) 2004; 15 Allen (CR35) 2009; 113 Tapon, Hall (CR21) 1997; 9 Zhang (CR6) 2005; 437 Liou (CR7) 2005; 15 Brown, West, Turner (CR31) 2002; 13 Nuche-Berenguer, Jensen (CR37) 2015; 1853 Soboloff, Madesh, Gill (CR42) 2011; 7 Grigoriev (CR9) 2008; 18 Che (CR20) 2015; 309 Zhao, Manser (CR27) 2005; 386 Aslan (CR34) 2013; 305 Abo (CR30) 1998; 17 Moccia (CR5) 2015; 9 Kim (CR39) 2016; 48 Casas-Rua (CR19) 2015; 1853 Delorme-Walker (CR33) 2011; 193 Daniels, Bokoch (CR22) 1999; 24 Tomas-Martin, Lopez-Guerrero, Casas-Rua, Pozo-Guisado, Martin-Romero (CR43) 2015; 27 Bishop, Hall (CR26) 2000; 1 Zhu (CR17) 2014; 33 Honnappa (CR11) 2009; 138 Hall (CR23) 2005; 33 Marchant (CR1) 2005; 15 Xu (CR15) 2015; 5 Wang (CR16) 2015; 34 Collins, Meyer (CR3) 2011; 21 Jermy (CR10) 2008; 10 Bustelo, Sauzeau, Berenjeno (CR24) 2007; 29 Itakura (CR29) 2013; 8 Galan, Dionisio, Smani, Salido, Rosado (CR14) 2011; 82 Kosoff, Chow, Radu, Chernoff (CR36) 2013; 288 Wang (CR38) 2014; 7 Cahalan (CR2) 2007; 42 Kim (CR18) 2014; 448 Loo, Ng, Lim, Manser (CR32) 2004; 24 Okeke, Dingsdale, Parker, Voronina, Tepikin (CR12) 2016; 594 Parrini, Matsuda, de Gunzburg (CR41) 2005; 33 Prakriya, Lewis (CR4) 2015; 95 Sells (CR25) 1997; 7 Patterson, van Rossum, Gill (CR13) 1999; 98 Lee (CR8) 2013; 35 Eby (CR40) 1998; 8 MC Brown (93_CR31) 2002; 13 J Soboloff (93_CR42) 2011; 7 J Liou (93_CR7) 2005; 15 JE Aslan (93_CR34) 2013; 305 V Casas-Rua (93_CR19) 2015; 1853 MR Stofega (93_CR28) 2004; 15 MD Cahalan (93_CR2) 2007; 42 A Jermy (93_CR10) 2008; 10 C Galan (93_CR14) 2011; 82 DJ Kim (93_CR39) 2016; 48 TH Loo (93_CR32) 2004; 24 JS Marchant (93_CR1) 2005; 15 SL Zhang (93_CR6) 2005; 437 VD Delorme-Walker (93_CR33) 2011; 193 N Tapon (93_CR21) 1997; 9 A Abo (93_CR30) 1998; 17 JJ Eby (93_CR40) 1998; 8 F Moccia (93_CR5) 2015; 9 RL Patterson (93_CR13) 1999; 98 ZS Zhao (93_CR27) 2005; 386 MC Parrini (93_CR41) 2005; 33 JH Kim (93_CR18) 2014; 448 A Hall (93_CR23) 2005; 33 SR Collins (93_CR3) 2011; 21 Y Wang (93_CR38) 2014; 7 RH Daniels (93_CR22) 1999; 24 B Nuche-Berenguer (93_CR37) 2015; 1853 H Che (93_CR20) 2015; 309 A Itakura (93_CR29) 2013; 8 JE Lee (93_CR8) 2013; 35 I Grigoriev (93_CR9) 2008; 18 S Honnappa (93_CR11) 2009; 138 JY Wang (93_CR16) 2015; 34 R Kosoff (93_CR36) 2013; 288 E Okeke (93_CR12) 2016; 594 XR Bustelo (93_CR24) 2007; 29 M Zhu (93_CR17) 2014; 33 JD Allen (93_CR35) 2009; 113 M Prakriya (93_CR4) 2015; 95 MA Sells (93_CR25) 1997; 7 P Tomas-Martin (93_CR43) 2015; 27 Y Xu (93_CR15) 2015; 5 AL Bishop (93_CR26) 2000; 1 |
| References_xml | – volume: 15 start-page: R493 year: 2005 end-page: R495 ident: CR1 article-title: Cellular signalling: STIMulating calcium entry publication-title: Curr. Biol. – volume: 17 start-page: 6527 year: 1998 end-page: 6540 ident: CR30 article-title: PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia publication-title: EMBO J. – volume: 35 start-page: 41 year: 2013 end-page: 46 ident: CR8 article-title: Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization publication-title: Mol. Cells – volume: 138 start-page: 366 year: 2009 end-page: 376 ident: CR11 article-title: An EB1-binding motif acts as a microtubule tip localization signal publication-title: Cell – volume: 437 start-page: 902 year: 2005 end-page: 905 ident: CR6 article-title: STIM1 is a Ca sensor that activates CRAC channels and migrates from the Ca store to the plasma membrane publication-title: Nature – volume: 33 start-page: 646 year: 2005 end-page: 648 ident: CR41 article-title: Spatiotemporal regulation of the Pak1 kinase publication-title: Biochem. Soc. Trans. – volume: 448 start-page: 76 year: 2014 end-page: 82 ident: CR18 article-title: Orai1 and STIM1 are critical for cell migration and proliferation of clear cell renal cell carcinoma publication-title: Biochem. Biophys. Res. Commun. – volume: 33 start-page: 891 year: 2005 end-page: 895 ident: CR23 article-title: Rho GTPases and the control of cell behaviour publication-title: Biochem. Soc. Trans. – volume: 193 start-page: 1289 year: 2011 end-page: 1303 ident: CR33 article-title: Pak1 regulates focal adhesion strength, myosin IIA distribution, and actin dynamics to optimize cell migration publication-title: J. Cell Biol. – volume: 9 start-page: 153 year: 2015 ident: CR5 article-title: Stim and Orai proteins in neuronal Ca ( ) signaling and excitability publication-title: Front. Cell. Neurosci. – volume: 15 start-page: 1235 year: 2005 end-page: 1241 ident: CR7 article-title: STIM is a Ca sensor essential for Ca -store-depletion-triggered Ca influx publication-title: Curr. Biol. – volume: 34 start-page: 4358 year: 2015 end-page: 4367 ident: CR16 article-title: STIM1 overexpression promotes colorectal cancer progression, cell motility and COX-2 expression publication-title: Oncogene – volume: 288 start-page: 974 year: 2013 end-page: 983 ident: CR36 article-title: Pak2 kinase restrains mast cell FcεRI receptor signaling through modulation of Rho protein guanine nucleotide exchange factor (GEF) activity publication-title: J. Biol. Chem. – volume: 18 start-page: 177 year: 2008 end-page: 182 ident: CR9 article-title: STIM1 is a MT-plus-end-tracking protein involved in remodeling of the ER publication-title: Curr. Biol. – volume: 15 start-page: 2965 year: 2004 end-page: 2977 ident: CR28 article-title: Constitutive p21-activated kinase (PAK) activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions publication-title: Mol. Biol. Cell – volume: 9 start-page: 86 year: 1997 end-page: 92 ident: CR21 article-title: Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton publication-title: Curr. Opin. Cell Biol. – volume: 7 start-page: 938 year: 2014 end-page: 948 ident: CR38 article-title: Pak1 is required to maintain ventricular Ca( ) homeostasis and electrophysiological stability through SERCA2a regulation in mice publication-title: Circ. Arrhythm. Electrophysiol. – volume: 48 year: 2016 ident: CR39 article-title: Small molecules that allosterically inhibit p21-activated kinase activity by binding to the regulatory p21-binding domain publication-title: Exp. Mol. Med. – volume: 7 start-page: 488 year: 2011 end-page: 492 ident: CR42 article-title: Sensing cellular stress through STIM proteins publication-title: Nat. Chem. Biol. – volume: 13 start-page: 1550 year: 2002 end-page: 1565 ident: CR31 article-title: Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway publication-title: Mol. Biol. Cell – volume: 1 start-page: 241 year: 2000 end-page: 255 ident: CR26 article-title: Rho GTPases and their effector proteins publication-title: Biochem. J. – volume: 386 start-page: 201 year: 2005 end-page: 214 ident: CR27 article-title: PAK and other Rho-associated kinases--effectors with surprisingly diverse mechanisms of regulation publication-title: Biochem. J. – volume: 309 start-page: 1772 year: 2015 end-page: 1781 ident: CR20 article-title: Roles of store-operated Ca channels in regulating cell cycling and migration of human cardiac c-kit + progenitor cells publication-title: Am. J. Physiol. Heart Circ. Physiol. – volume: 8 start-page: 967 year: 1998 end-page: 970 ident: CR40 article-title: Actin cytoskeleton organization regulated by the PAK family of protein kinases publication-title: Curr. Biol. – volume: 1853 start-page: 2371 year: 2015 end-page: 2382 ident: CR37 article-title: Gastrointestinal hormones/neurotransmitters and growth factors can activate P21 activated kinase 2 in pancreatic acinar cells by novel mechanisms publication-title: Biochim. Biophys. Acta – volume: 5 year: 2015 ident: CR15 article-title: STIM1 accelerates cell senescence in a remodeled microenvironment but enhances the epithelial-to-mesenchymal transition in prostate cancer publication-title: Sci. Rep. – volume: 33 start-page: 98 year: 2014 ident: CR17 article-title: Store-operated Ca( ) entry regulates glioma cell migration and invasion via modulation of Pyk2 phosphorylation publication-title: J. Exp. Clin. Cancer Res. – volume: 21 start-page: 202 year: 2011 end-page: 211 ident: CR3 article-title: Evolutionary origins of STIM1 and STIM2 within ancient Ca signaling systems publication-title: Trends Cell Biol. – volume: 10 start-page: 384 year: 2008 ident: CR10 article-title: STIM1 tracks growing microtubule ends publication-title: Nat. Cell. Biol. – volume: 305 start-page: C519 year: 2013 end-page: C528 ident: CR34 article-title: The PAK system links Rho GTPase signaling to thrombin-mediated platelet activation publication-title: Am. J. Physiol. Cell Physiol. – volume: 95 start-page: 1383 year: 2015 end-page: 1436 ident: CR4 article-title: Store-operated calcium channels publication-title: Physiol. Rev. – volume: 8 start-page: e73063 year: 2013 ident: CR29 article-title: p21-Activated kinase (PAK) regulates cytoskeletal reorganization and directional migration in human neutrophils publication-title: PLoS ONE – volume: 98 start-page: 487 year: 1999 end-page: 499 ident: CR13 article-title: Store-operated Ca21 entry evidence for a secretion-like coupling model publication-title: Cell – volume: 7 start-page: 202 year: 1997 end-page: 210 ident: CR25 article-title: Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells publication-title: Curr. Biol. – volume: 594 start-page: 2837 year: 2016 end-page: 2847 ident: CR12 article-title: Endoplasmic reticulum-plasma membrane junctions: structure, function and dynamics publication-title: J. Physiol. – volume: 29 start-page: 356 year: 2007 end-page: 370 ident: CR24 article-title: GTP-binding proteins of the Rho Rac family regulation, effectors and functions in vivo publication-title: Bioessays – volume: 24 start-page: 3849 year: 2004 end-page: 3859 ident: CR32 article-title: GIT1 activates p21-activated kinase through a mechanism independent of p21 binding publication-title: Mol. Cell. Biol. – volume: 113 start-page: 2695 year: 2009 end-page: 2705 ident: CR35 article-title: p21- activated kinase regulates mast cell degranulation via effects on calcium mobilization and cytoskeletal dynamics publication-title: Blood – volume: 1853 start-page: 233 year: 2015 end-page: 243 ident: CR19 article-title: STIM1 phosphorylation triggered by epidermal growth factor mediates cell migration publication-title: Biochim. Biophys. Acta – volume: 27 start-page: 545 year: 2015 end-page: 554 ident: CR43 article-title: Phospho-STIM1 is a downstream effector that mediates the signaling triggered by IGF-1 in HEK293 cells publication-title: Cell. Signal. – volume: 82 start-page: 400 year: 2011 end-page: 410 ident: CR14 article-title: The cytoskeleton plays a modulatory role in the association between STIM1 and the Ca channel subunits Orai1 and TRPC1 publication-title: Biochem. Pharmacol. – volume: 24 start-page: 350 year: 1999 end-page: 355 ident: CR22 article-title: p21-Activated protein kinase- a crucial component of morphological signaling publication-title: Trends Biochem. Sci. – volume: 42 start-page: 133 year: 2007 end-page: 144 ident: CR2 article-title: Molecular basis of the CRAC channel publication-title: Cell Calcium – volume: 21 start-page: 202 year: 2011 ident: 93_CR3 publication-title: Trends Cell Biol. doi: 10.1016/j.tcb.2011.01.002 – volume: 24 start-page: 350 year: 1999 ident: 93_CR22 publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(99)01442-5 – volume: 17 start-page: 6527 year: 1998 ident: 93_CR30 publication-title: EMBO J. doi: 10.1093/emboj/17.22.6527 – volume: 15 start-page: 1235 year: 2005 ident: 93_CR7 publication-title: Curr. Biol. doi: 10.1016/j.cub.2005.05.055 – volume: 305 start-page: C519 year: 2013 ident: 93_CR34 publication-title: Am. J. Physiol. Cell Physiol. doi: 10.1152/ajpcell.00418.2012 – volume: 7 start-page: 202 year: 1997 ident: 93_CR25 publication-title: Curr. Biol. doi: 10.1016/S0960-9822(97)70091-5 – volume: 33 start-page: 891 year: 2005 ident: 93_CR23 publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0330891 – volume: 34 start-page: 4358 year: 2015 ident: 93_CR16 publication-title: Oncogene doi: 10.1038/onc.2014.366 – volume: 9 start-page: 86 year: 1997 ident: 93_CR21 publication-title: Curr. Opin. Cell Biol. doi: 10.1016/S0955-0674(97)80156-1 – volume: 15 start-page: 2965 year: 2004 ident: 93_CR28 publication-title: Mol. Biol. Cell doi: 10.1091/mbc.e03-08-0604 – volume: 7 start-page: 488 year: 2011 ident: 93_CR42 publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.619 – volume: 42 start-page: 133 year: 2007 ident: 93_CR2 publication-title: Cell Calcium doi: 10.1016/j.ceca.2007.03.002 – volume: 24 start-page: 3849 year: 2004 ident: 93_CR32 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.24.9.3849-3859.2004 – volume: 594 start-page: 2837 year: 2016 ident: 93_CR12 publication-title: J. Physiol. doi: 10.1113/JP271142 – volume: 18 start-page: 177 year: 2008 ident: 93_CR9 publication-title: Curr. Biol. doi: 10.1016/j.cub.2007.12.050 – volume: 437 start-page: 902 year: 2005 ident: 93_CR6 publication-title: Nature doi: 10.1038/nature04147 – volume: 10 start-page: 384 year: 2008 ident: 93_CR10 publication-title: Nat. Cell. Biol. doi: 10.1038/ncb0408-384 – volume: 1853 start-page: 2371 year: 2015 ident: 93_CR37 publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2015.05.011 – volume: 288 start-page: 974 year: 2013 ident: 93_CR36 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.422295 – volume: 33 start-page: 646 year: 2005 ident: 93_CR41 publication-title: Biochem. Soc. Trans. doi: 10.1042/BST0330646 – volume: 27 start-page: 545 year: 2015 ident: 93_CR43 publication-title: Cell. Signal. doi: 10.1016/j.cellsig.2014.12.017 – volume: 33 start-page: 98 year: 2014 ident: 93_CR17 publication-title: J. Exp. Clin. Cancer Res. – volume: 35 start-page: 41 year: 2013 ident: 93_CR8 publication-title: Mol. Cells doi: 10.1007/s10059-013-2268-7 – volume: 138 start-page: 366 year: 2009 ident: 93_CR11 publication-title: Cell doi: 10.1016/j.cell.2009.04.065 – volume: 98 start-page: 487 year: 1999 ident: 93_CR13 publication-title: Cell doi: 10.1016/S0092-8674(00)81977-7 – volume: 8 start-page: 967 year: 1998 ident: 93_CR40 publication-title: Curr. Biol. doi: 10.1016/S0960-9822(98)00398-4 – volume: 1 start-page: 241 year: 2000 ident: 93_CR26 publication-title: Biochem. J. doi: 10.1042/bj3480241 – volume: 9 start-page: 153 year: 2015 ident: 93_CR5 publication-title: Front. Cell. Neurosci. doi: 10.3389/fncel.2015.00153 – volume: 193 start-page: 1289 year: 2011 ident: 93_CR33 publication-title: J. Cell Biol. doi: 10.1083/jcb.201010059 – volume: 113 start-page: 2695 year: 2009 ident: 93_CR35 publication-title: Blood doi: 10.1182/blood-2008-06-160861 – volume: 448 start-page: 76 year: 2014 ident: 93_CR18 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2014.04.064 – volume: 386 start-page: 201 year: 2005 ident: 93_CR27 publication-title: Biochem. J. doi: 10.1042/BJ20041638 – volume: 15 start-page: R493 year: 2005 ident: 93_CR1 publication-title: Curr. Biol. doi: 10.1016/j.cub.2005.06.035 – volume: 8 start-page: e73063 year: 2013 ident: 93_CR29 publication-title: PLoS ONE doi: 10.1371/journal.pone.0073063 – volume: 48 year: 2016 ident: 93_CR39 publication-title: Exp. Mol. Med. – volume: 309 start-page: 1772 year: 2015 ident: 93_CR20 publication-title: Am. J. Physiol. Heart Circ. Physiol. doi: 10.1152/ajpheart.00260.2015 – volume: 5 year: 2015 ident: 93_CR15 publication-title: Sci. Rep. – volume: 29 start-page: 356 year: 2007 ident: 93_CR24 publication-title: Bioessays doi: 10.1002/bies.20558 – volume: 13 start-page: 1550 year: 2002 ident: 93_CR31 publication-title: Mol. Biol. Cell doi: 10.1091/mbc.02-02-0015 – volume: 95 start-page: 1383 year: 2015 ident: 93_CR4 publication-title: Physiol. Rev. doi: 10.1152/physrev.00020.2014 – volume: 1853 start-page: 233 year: 2015 ident: 93_CR19 publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2014.10.027 – volume: 82 start-page: 400 year: 2011 ident: 93_CR14 publication-title: Biochem. Pharmacol. doi: 10.1016/j.bcp.2011.05.017 – volume: 7 start-page: 938 year: 2014 ident: 93_CR38 publication-title: Circ. Arrhythm. Electrophysiol. doi: 10.1161/CIRCEP.113.001198 |
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| Snippet | Calcium mobilization is necessary for cell movement during embryonic development, lymphocyte synapse formation, wound healing, and cancer cell metastasis.... Calcium mobilization is necessary for cell movement during embryonicdevelopment, lymphocyte synapse formation, wound healing, and cancer cellmetastasis.... Cancer: Mediating metastatic migration A molecular mechanism underlying cell movement may contribute to the aggressive migration of metastatic tumor cells. A... |
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| SubjectTerms | 14 14/19 631/80/79/2027 631/80/86/1999 82 96 Biomedical and Life Sciences Biomedicine Calcium - metabolism Calcium channels Calcium influx Calcium mobilization Cancer Cell Adhesion Cell adhesion & migration Cell Surface Extensions - metabolism Cytoskeleton Cytosol Embryogenesis Endoplasmic reticulum HEK293 Cells HeLa Cells Humans Inositol trisphosphate Intracellular Space - metabolism Leukocyte migration Localization Medical Biochemistry Metastases Metastasis Molecular Medicine Neoplasm Proteins - metabolism Oligomerization Orai1 protein p21-activated kinase p21-Activated Kinases - metabolism Phosphorylation Protein Binding Stem Cells STIM1 protein Stromal Interaction Molecule 1 - metabolism Synapses Synaptogenesis Thapsigargin Vinculin Vinculin - metabolism Wound healing 생화학 |
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| Title | Modulation of store-operated calcium entry and nascent adhesion by p21-activated kinase 1 |
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