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Signaling from Rho to the Actin Cytoskeleton Through Protein Kinases ROCK and LIM-kinase
The actin cytoskeleton undergoes extensive remodeling during cell morphogenesis and motility. The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a resul...
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| Published in: | Science (American Association for the Advancement of Science) 1999-08, Vol.285 (5429), p.895-898 |
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| cites | cdi_FETCH-LOGICAL-c752t-5cb1d201c46e67985addbf7b28ad60b4135f90e3bce2eb1d46d87a317c2229ee3 |
| container_end_page | 898 |
| container_issue | 5429 |
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| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 285 |
| creator | Maekawa, Midori Ishizaki, Toshimasa Boku, Shuken Watanabe, Naoki Fujita, Akiko Iwamatsu, Akihiro Obinata, Takashi Ohashi, Kazumasa Mizuno, Kensaku Narumiya, Shuh |
| description | The actin cytoskeleton undergoes extensive remodeling during cell morphogenesis and motility. The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a result of its phosphorylation by LIM-kinase. Cofilin was phosphorylated in N1E-115 neuroblastoma cells during lysophosphatidic acid-induced, Rho-mediated neurite retraction. This phosphorylation was sensitive to Y-27632, a specific inhibitor of the Rho-associated kinase ROCK. ROCK, which is a downstream effector of Rho, did not phosphorylate cofilin directly but phosphorylated LIM-kinase, which in turn was activated to phosphorylate cofilin. Overexpression of LIM-kinase in HeLa cells induced the formation of actin stress fibers in a Y-27632-sensitive manner. These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton. |
| doi_str_mv | 10.1126/science.285.5429.895 |
| format | article |
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The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a result of its phosphorylation by LIM-kinase. Cofilin was phosphorylated in N1E-115 neuroblastoma cells during lysophosphatidic acid-induced, Rho-mediated neurite retraction. This phosphorylation was sensitive to Y-27632, a specific inhibitor of the Rho-associated kinase ROCK. ROCK, which is a downstream effector of Rho, did not phosphorylate cofilin directly but phosphorylated LIM-kinase, which in turn was activated to phosphorylate cofilin. Overexpression of LIM-kinase in HeLa cells induced the formation of actin stress fibers in a Y-27632-sensitive manner. These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.285.5429.895</identifier><identifier>PMID: 10436159</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Actin ; Actin Cytoskeleton - metabolism ; Actin Depolymerizing Factors ; Actins ; Actins - metabolism ; Amides - pharmacology ; Animals ; Antibodies ; Biological and medical sciences ; Cell structures and functions ; Cellular biology ; COS Cells ; Cytoskeleton ; Cytoskeleton, cytoplasm. Intracellular movements ; DNA-Binding Proteins - metabolism ; Enzyme Activation ; Fundamental and applied biological sciences. 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These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton.</description><subject>Actin</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Actin Depolymerizing Factors</subject><subject>Actins</subject><subject>Actins - metabolism</subject><subject>Amides - pharmacology</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Cellular biology</subject><subject>COS Cells</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton, cytoplasm. Intracellular movements</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. 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Ishizaki, Toshimasa ; Boku, Shuken ; Watanabe, Naoki ; Fujita, Akiko ; Iwamatsu, Akihiro ; Obinata, Takashi ; Ohashi, Kazumasa ; Mizuno, Kensaku ; Narumiya, Shuh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c752t-5cb1d201c46e67985addbf7b28ad60b4135f90e3bce2eb1d46d87a317c2229ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Actin</topic><topic>Actin Cytoskeleton - metabolism</topic><topic>Actin Depolymerizing Factors</topic><topic>Actins</topic><topic>Actins - metabolism</topic><topic>Amides - pharmacology</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Cellular biology</topic><topic>COS Cells</topic><topic>Cytoskeleton</topic><topic>Cytoskeleton, cytoplasm. Intracellular movements</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Lim Kinases</topic><topic>Lysophospholipids - pharmacology</topic><topic>Membrane Proteins - metabolism</topic><topic>Microfilament Proteins - metabolism</topic><topic>Microfilaments</topic><topic>Molecular and cellular biology</topic><topic>Morphogenesis</topic><topic>Neurites</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Protein Kinases - metabolism</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteins</topic><topic>Pyridines - pharmacology</topic><topic>rho-Associated Kinases</topic><topic>rhoB GTP-Binding Protein</topic><topic>Signal Transduction</topic><topic>Stimuli</topic><topic>Stress fibers</topic><topic>Tumor Cells, 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Science)</jtitle><addtitle>Science</addtitle><date>1999-08-06</date><risdate>1999</risdate><volume>285</volume><issue>5429</issue><spage>895</spage><epage>898</epage><pages>895-898</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The actin cytoskeleton undergoes extensive remodeling during cell morphogenesis and motility. The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a result of its phosphorylation by LIM-kinase. Cofilin was phosphorylated in N1E-115 neuroblastoma cells during lysophosphatidic acid-induced, Rho-mediated neurite retraction. This phosphorylation was sensitive to Y-27632, a specific inhibitor of the Rho-associated kinase ROCK. ROCK, which is a downstream effector of Rho, did not phosphorylate cofilin directly but phosphorylated LIM-kinase, which in turn was activated to phosphorylate cofilin. Overexpression of LIM-kinase in HeLa cells induced the formation of actin stress fibers in a Y-27632-sensitive manner. These results indicate that phosphorylation of LIM-kinase by ROCK and consequently increased phosphorylation of cofilin by LIM-kinase contribute to Rho-induced reorganization of the actin cytoskeleton.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>10436159</pmid><doi>10.1126/science.285.5429.895</doi><tpages>4</tpages></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1999-08, Vol.285 (5429), p.895-898 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743744361 |
| source | Science Magazine; JSTOR Archival Journals and Primary Sources Collection; Social Science Premium Collection; Alma/SFX Local Collection; Education Collection |
| subjects | Actin Actin Cytoskeleton - metabolism Actin Depolymerizing Factors Actins Actins - metabolism Amides - pharmacology Animals Antibodies Biological and medical sciences Cell structures and functions Cellular biology COS Cells Cytoskeleton Cytoskeleton, cytoplasm. Intracellular movements DNA-Binding Proteins - metabolism Enzyme Activation Fundamental and applied biological sciences. Psychology Gels GTP Phosphohydrolases - metabolism GTP-Binding Proteins - metabolism HeLa Cells Humans Intracellular Signaling Peptides and Proteins Lim Kinases Lysophospholipids - pharmacology Membrane Proteins - metabolism Microfilament Proteins - metabolism Microfilaments Molecular and cellular biology Morphogenesis Neurites Phosphorylation Physiological aspects Protein Kinases - metabolism Protein-Serine-Threonine Kinases - metabolism Proteins Pyridines - pharmacology rho-Associated Kinases rhoB GTP-Binding Protein Signal Transduction Stimuli Stress fibers Tumor Cells, Cultured |
| title | Signaling from Rho to the Actin Cytoskeleton Through Protein Kinases ROCK and LIM-kinase |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T17%3A09%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Signaling%20from%20Rho%20to%20the%20Actin%20Cytoskeleton%20Through%20Protein%20Kinases%20ROCK%20and%20LIM-kinase&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Maekawa,%20Midori&rft.date=1999-08-06&rft.volume=285&rft.issue=5429&rft.spage=895&rft.epage=898&rft.pages=895-898&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.285.5429.895&rft_dat=%3Cgale_proqu%3EA55578474%3C/gale_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c752t-5cb1d201c46e67985addbf7b28ad60b4135f90e3bce2eb1d46d87a317c2229ee3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=213590472&rft_id=info:pmid/10436159&rft_galeid=A55578474&rft_jstor_id=2898603&rfr_iscdi=true |