Regulation of Cofilin Activity by CaMKII and Calcineurin
Abstract Cofilin promotes actin filament turnover by severing and depolymerizing actin filaments. Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca2+ -...
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| Veröffentlicht in: | The American journal of the medical sciences 2012-12, Vol.344 (6), p.462-472 |
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| creator | Zhao, Jian-Wu, MD, PhD Gao, Zhong-Li, MD Zhang, Han-Yang, MD Ji, Qiu-Ye, MS Wang, Hong, MD, PhD Yang, Yu-Dan, MD, PhD Xing, Feng-juan, MD Meng, Ling-jie, MD, PhD Wang, Yan, MD, PhD |
| description | Abstract Cofilin promotes actin filament turnover by severing and depolymerizing actin filaments. Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca2+ -induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca2+ /calmodulin-dependent protein kinase II (CaMKII) is shown to negatively regulate SSH1L activity and bind to SSH1L in a complex with 14-3-3. Phosphorylation of LIMK1 by CaMKII and its subsequent activation regulates the subcellular localization of SSH1L. Based on these findings, the authors suggest that CaMKII and Cn provide a switch-like mechanism that controls Ca2+ -dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization. |
| doi_str_mv | 10.1097/MAJ.0b013e318244745b |
| format | Article |
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Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca2+ -induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca2+ /calmodulin-dependent protein kinase II (CaMKII) is shown to negatively regulate SSH1L activity and bind to SSH1L in a complex with 14-3-3. Phosphorylation of LIMK1 by CaMKII and its subsequent activation regulates the subcellular localization of SSH1L. Based on these findings, the authors suggest that CaMKII and Cn provide a switch-like mechanism that controls Ca2+ -dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization.</description><identifier>ISSN: 0002-9629</identifier><identifier>EISSN: 1538-2990</identifier><identifier>DOI: 10.1097/MAJ.0b013e318244745b</identifier><identifier>PMID: 22270398</identifier><identifier>CODEN: AJMSA9</identifier><language>eng</language><publisher>Hagerstown, MD: Elsevier Inc</publisher><subject>14-3-3 Proteins - metabolism ; Actin Cytoskeleton - chemistry ; Actin Cytoskeleton - metabolism ; Biological and medical sciences ; Calcimycin - pharmacology ; Calcineurin (Cn) ; Calcineurin - metabolism ; Calcium - metabolism ; Calcium Ionophores - pharmacology ; Calcium-calmodulin-dependent protein kinase II (CaMKII) ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism ; Cofilin 1 - metabolism ; Cofilin activity ; Enzyme Activation - drug effects ; Gene Knockdown Techniques ; General aspects ; HEK293 Cells ; Humans ; Internal Medicine ; Lim Kinases - antagonists & inhibitors ; Lim Kinases - genetics ; Lim Kinases - metabolism ; MCF-7 Cells ; Medical sciences ; Models, Biological ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Phosphoprotein Phosphatases - genetics ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; Protein Binding ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Serine - chemistry ; Signal Transduction</subject><ispartof>The American journal of the medical sciences, 2012-12, Vol.344 (6), p.462-472</ispartof><rights>Southern Society for Clinical Investigation</rights><rights>2012 Southern Society for Clinical Investigation</rights><rights>2014 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c564t-89cbd6dcf0b2b7d5fb15da492a9d31610a13b06087dae77d8d0d56c2c617c423</citedby><cites>FETCH-LOGICAL-c564t-89cbd6dcf0b2b7d5fb15da492a9d31610a13b06087dae77d8d0d56c2c617c423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26720673$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22270398$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Jian-Wu, MD, PhD</creatorcontrib><creatorcontrib>Gao, Zhong-Li, MD</creatorcontrib><creatorcontrib>Zhang, Han-Yang, MD</creatorcontrib><creatorcontrib>Ji, Qiu-Ye, MS</creatorcontrib><creatorcontrib>Wang, Hong, MD, PhD</creatorcontrib><creatorcontrib>Yang, Yu-Dan, MD, PhD</creatorcontrib><creatorcontrib>Xing, Feng-juan, MD</creatorcontrib><creatorcontrib>Meng, Ling-jie, MD, PhD</creatorcontrib><creatorcontrib>Wang, Yan, MD, PhD</creatorcontrib><title>Regulation of Cofilin Activity by CaMKII and Calcineurin</title><title>The American journal of the medical sciences</title><addtitle>Am J Med Sci</addtitle><description>Abstract Cofilin promotes actin filament turnover by severing and depolymerizing actin filaments. Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca2+ -induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca2+ /calmodulin-dependent protein kinase II (CaMKII) is shown to negatively regulate SSH1L activity and bind to SSH1L in a complex with 14-3-3. Phosphorylation of LIMK1 by CaMKII and its subsequent activation regulates the subcellular localization of SSH1L. Based on these findings, the authors suggest that CaMKII and Cn provide a switch-like mechanism that controls Ca2+ -dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization.</description><subject>14-3-3 Proteins - metabolism</subject><subject>Actin Cytoskeleton - chemistry</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Biological and medical sciences</subject><subject>Calcimycin - pharmacology</subject><subject>Calcineurin (Cn)</subject><subject>Calcineurin - metabolism</subject><subject>Calcium - metabolism</subject><subject>Calcium Ionophores - pharmacology</subject><subject>Calcium-calmodulin-dependent protein kinase II (CaMKII)</subject><subject>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism</subject><subject>Cofilin 1 - metabolism</subject><subject>Cofilin activity</subject><subject>Enzyme Activation - drug effects</subject><subject>Gene Knockdown Techniques</subject><subject>General aspects</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Lim Kinases - antagonists & inhibitors</subject><subject>Lim Kinases - genetics</subject><subject>Lim Kinases - metabolism</subject><subject>MCF-7 Cells</subject><subject>Medical sciences</subject><subject>Models, Biological</subject><subject>Phosphoprotein Phosphatases - antagonists & inhibitors</subject><subject>Phosphoprotein Phosphatases - genetics</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Serine - chemistry</subject><subject>Signal Transduction</subject><issn>0002-9629</issn><issn>1538-2990</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtrFEEURgtRzCT6D0R6I7jpeKuqux4bYRjUjCYImn1Rj9tSsac6VnUH5t9bw4wK2bi6d3Hug_MR8orCJQUt392sP1-CA8qRU8W6Tna9e0JWtOeqZVrDU7ICANZqwfQZOS_lDoAyRflzcsYYk8C1WhH1DX8so53jlJppaDbTEMeYmrWf40Oc943bNxt782W7bWwKtR19TLjkmF6QZ4MdC7481Qty-_HD7eaqvf76abtZX7e-F93cKu1dEMEP4JiToR8c7YPtNLM6cCooWModCFAyWJQyqAChF555QaXvGL8gb49r7_P0a8Eym10sHsfRJpyWYihjIHWv1QHtjqjPUykZB3Of487mvaFgDspMVWYeK6tjr08XFrfD8Hfoj6MKvDkBtng7DtkmH8s_TkgGQvLKvT9yWHU8RMym-IjJY4gZ_WzCFP_3yeMFvmYR682fuMdyNy05VdWGmsIMmO-HeA_p1shBKtnx333Em_I</recordid><startdate>20121201</startdate><enddate>20121201</enddate><creator>Zhao, Jian-Wu, MD, PhD</creator><creator>Gao, Zhong-Li, MD</creator><creator>Zhang, Han-Yang, MD</creator><creator>Ji, Qiu-Ye, MS</creator><creator>Wang, Hong, MD, PhD</creator><creator>Yang, Yu-Dan, MD, PhD</creator><creator>Xing, Feng-juan, MD</creator><creator>Meng, Ling-jie, MD, PhD</creator><creator>Wang, Yan, MD, PhD</creator><general>Elsevier Inc</general><general>Lippincott Williams & Wilkins</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20121201</creationdate><title>Regulation of Cofilin Activity by CaMKII and Calcineurin</title><author>Zhao, Jian-Wu, MD, PhD ; Gao, Zhong-Li, MD ; Zhang, Han-Yang, MD ; Ji, Qiu-Ye, MS ; Wang, Hong, MD, PhD ; Yang, Yu-Dan, MD, PhD ; Xing, Feng-juan, MD ; Meng, Ling-jie, MD, PhD ; Wang, Yan, MD, PhD</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c564t-89cbd6dcf0b2b7d5fb15da492a9d31610a13b06087dae77d8d0d56c2c617c423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>14-3-3 Proteins - metabolism</topic><topic>Actin Cytoskeleton - chemistry</topic><topic>Actin Cytoskeleton - metabolism</topic><topic>Biological and medical sciences</topic><topic>Calcimycin - pharmacology</topic><topic>Calcineurin (Cn)</topic><topic>Calcineurin - metabolism</topic><topic>Calcium - metabolism</topic><topic>Calcium Ionophores - pharmacology</topic><topic>Calcium-calmodulin-dependent protein kinase II (CaMKII)</topic><topic>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism</topic><topic>Cofilin 1 - metabolism</topic><topic>Cofilin activity</topic><topic>Enzyme Activation - drug effects</topic><topic>Gene Knockdown Techniques</topic><topic>General aspects</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Internal Medicine</topic><topic>Lim Kinases - antagonists & inhibitors</topic><topic>Lim Kinases - genetics</topic><topic>Lim Kinases - metabolism</topic><topic>MCF-7 Cells</topic><topic>Medical sciences</topic><topic>Models, Biological</topic><topic>Phosphoprotein Phosphatases - antagonists & inhibitors</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Serine - chemistry</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Jian-Wu, MD, PhD</creatorcontrib><creatorcontrib>Gao, Zhong-Li, MD</creatorcontrib><creatorcontrib>Zhang, Han-Yang, MD</creatorcontrib><creatorcontrib>Ji, Qiu-Ye, MS</creatorcontrib><creatorcontrib>Wang, Hong, MD, PhD</creatorcontrib><creatorcontrib>Yang, Yu-Dan, MD, PhD</creatorcontrib><creatorcontrib>Xing, Feng-juan, MD</creatorcontrib><creatorcontrib>Meng, Ling-jie, MD, PhD</creatorcontrib><creatorcontrib>Wang, Yan, MD, PhD</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The American journal of the medical sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Jian-Wu, MD, PhD</au><au>Gao, Zhong-Li, MD</au><au>Zhang, Han-Yang, MD</au><au>Ji, Qiu-Ye, MS</au><au>Wang, Hong, MD, PhD</au><au>Yang, Yu-Dan, MD, PhD</au><au>Xing, Feng-juan, MD</au><au>Meng, Ling-jie, MD, PhD</au><au>Wang, Yan, MD, PhD</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of Cofilin Activity by CaMKII and Calcineurin</atitle><jtitle>The American journal of the medical sciences</jtitle><addtitle>Am J Med Sci</addtitle><date>2012-12-01</date><risdate>2012</risdate><volume>344</volume><issue>6</issue><spage>462</spage><epage>472</epage><pages>462-472</pages><issn>0002-9629</issn><eissn>1538-2990</eissn><coden>AJMSA9</coden><abstract>Abstract Cofilin promotes actin filament turnover by severing and depolymerizing actin filaments. Cofilin is inactivated by phosphorylation on Ser-3 by LIM-kinase1 (LIMK1) and is activated when protein phosphatase Slingshot-1L (SSH1L) dephosphorylates this residue. The authors have shown that Ca2+ -induced cofilin dephosphorylation is mediated by calcineurin (Cn)-dependent activation of SSH1L. In this study, Ca2+ /calmodulin-dependent protein kinase II (CaMKII) is shown to negatively regulate SSH1L activity and bind to SSH1L in a complex with 14-3-3. Phosphorylation of LIMK1 by CaMKII and its subsequent activation regulates the subcellular localization of SSH1L. Based on these findings, the authors suggest that CaMKII and Cn provide a switch-like mechanism that controls Ca2+ -dependent LIMK1, SSH1L and cofilin activation, and subsequently actin cytoskeletal reorganization.</abstract><cop>Hagerstown, MD</cop><pub>Elsevier Inc</pub><pmid>22270398</pmid><doi>10.1097/MAJ.0b013e318244745b</doi><tpages>11</tpages></addata></record> |
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| subjects | 14-3-3 Proteins - metabolism Actin Cytoskeleton - chemistry Actin Cytoskeleton - metabolism Biological and medical sciences Calcimycin - pharmacology Calcineurin (Cn) Calcineurin - metabolism Calcium - metabolism Calcium Ionophores - pharmacology Calcium-calmodulin-dependent protein kinase II (CaMKII) Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism Cofilin 1 - metabolism Cofilin activity Enzyme Activation - drug effects Gene Knockdown Techniques General aspects HEK293 Cells Humans Internal Medicine Lim Kinases - antagonists & inhibitors Lim Kinases - genetics Lim Kinases - metabolism MCF-7 Cells Medical sciences Models, Biological Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Phosphorylation Protein Binding Recombinant Proteins - genetics Recombinant Proteins - metabolism Serine - chemistry Signal Transduction |
| title | Regulation of Cofilin Activity by CaMKII and Calcineurin |
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