Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho- Kinase)
The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP·RhoA) specifically interacted with...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1996-07, Vol.273 (5272), p.245-248 |
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| creator | Kimura, Kazushi Ito, Masaaki Amano, Mutsuki Chihara, Kazuyasu Fukata, Yuko Nakafuku, Masato Yamamori, Bunpei Feng, Jianhua Nakano, Takeshi Okawa, Katsuya Iwamatsu, Akihiro Kaibuchi, Kozo |
| description | The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP·RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP·RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase. |
| doi_str_mv | 10.1126/science.273.5272.245 |
| format | Article |
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The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP·RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP·RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.273.5272.245</identifier><identifier>PMID: 8662509</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>3T3 Cells ; Actins - metabolism ; Amino Acid Sequence ; Amino acids ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Calcium ; Cattle ; Cell lines ; Cellular biology ; COS cells ; Enzymes and enzyme inhibitors ; Exhibits ; Fundamental and applied biological sciences. Psychology ; GTP Phosphohydrolases - metabolism ; GTP-Binding Proteins - metabolism ; GTPases ; Guanosine triphosphatase ; Hydrolases ; Intracellular Signaling Peptides and Proteins ; Isopropyl Thiogalactoside - pharmacology ; Literary Devices ; Mice ; Molecular Sequence Data ; Muscle Contraction ; Muscle, Smooth - physiology ; Myosin ; Myosin Light Chains - metabolism ; Myosin-Light-Chain Phosphatase ; NIH 3T3 cells ; Oxazoles - pharmacology ; Phosphatases ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; Physiological regulation ; Plasmids ; Protein kinases ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Rho(D) immune globulin ; rho-Associated Kinases ; rhoA GTP-Binding Protein ; Smooth muscle</subject><ispartof>Science (American Association for the Advancement of Science), 1996-07, Vol.273 (5272), p.245-248</ispartof><rights>Copyright 1996 American Association for the Advancement of Science</rights><rights>1996 INIST-CNRS</rights><rights>COPYRIGHT 1996 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Jul 12, 1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c809t-183b67ca6b65024001797920f45ec5a875bc1ae69fb2736222bdb526087f61a13</citedby><cites>FETCH-LOGICAL-c809t-183b67ca6b65024001797920f45ec5a875bc1ae69fb2736222bdb526087f61a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2890422$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2890422$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,777,781,800,2871,2872,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3159754$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8662509$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kimura, Kazushi</creatorcontrib><creatorcontrib>Ito, Masaaki</creatorcontrib><creatorcontrib>Amano, Mutsuki</creatorcontrib><creatorcontrib>Chihara, Kazuyasu</creatorcontrib><creatorcontrib>Fukata, Yuko</creatorcontrib><creatorcontrib>Nakafuku, Masato</creatorcontrib><creatorcontrib>Yamamori, Bunpei</creatorcontrib><creatorcontrib>Feng, Jianhua</creatorcontrib><creatorcontrib>Nakano, Takeshi</creatorcontrib><creatorcontrib>Okawa, Katsuya</creatorcontrib><creatorcontrib>Iwamatsu, Akihiro</creatorcontrib><creatorcontrib>Kaibuchi, Kozo</creatorcontrib><title>Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho- Kinase)</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP·RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP·RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.</description><subject>3T3 Cells</subject><subject>Actins - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium</subject><subject>Cattle</subject><subject>Cell lines</subject><subject>Cellular biology</subject><subject>COS cells</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Exhibits</subject><subject>Fundamental and applied biological sciences. 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metabolism</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium</topic><topic>Cattle</topic><topic>Cell lines</topic><topic>Cellular biology</topic><topic>COS cells</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Exhibits</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>GTPases</topic><topic>Guanosine triphosphatase</topic><topic>Hydrolases</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Isopropyl Thiogalactoside - pharmacology</topic><topic>Literary Devices</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Muscle Contraction</topic><topic>Muscle, Smooth - physiology</topic><topic>Myosin</topic><topic>Myosin Light Chains - metabolism</topic><topic>Myosin-Light-Chain Phosphatase</topic><topic>NIH 3T3 cells</topic><topic>Oxazoles - pharmacology</topic><topic>Phosphatases</topic><topic>Phosphoprotein Phosphatases - antagonists & inhibitors</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Physiological regulation</topic><topic>Plasmids</topic><topic>Protein kinases</topic><topic>Protein-Serine-Threonine Kinases - 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Rho and Rho-Associated Kinase (Rho- Kinase)</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1996-07-12</date><risdate>1996</risdate><volume>273</volume><issue>5272</issue><spage>245</spage><epage>248</epage><pages>245-248</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP·RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP·RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>8662509</pmid><doi>10.1126/science.273.5272.245</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1996-07, Vol.273 (5272), p.245-248 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743416117 |
| source | MEDLINE; American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | 3T3 Cells Actins - metabolism Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcium Cattle Cell lines Cellular biology COS cells Enzymes and enzyme inhibitors Exhibits Fundamental and applied biological sciences. Psychology GTP Phosphohydrolases - metabolism GTP-Binding Proteins - metabolism GTPases Guanosine triphosphatase Hydrolases Intracellular Signaling Peptides and Proteins Isopropyl Thiogalactoside - pharmacology Literary Devices Mice Molecular Sequence Data Muscle Contraction Muscle, Smooth - physiology Myosin Myosin Light Chains - metabolism Myosin-Light-Chain Phosphatase NIH 3T3 cells Oxazoles - pharmacology Phosphatases Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - metabolism Phosphorylation Physiological regulation Plasmids Protein kinases Protein-Serine-Threonine Kinases - metabolism Proteins Rho(D) immune globulin rho-Associated Kinases rhoA GTP-Binding Protein Smooth muscle |
| title | Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho- Kinase) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T20%3A59%3A18IST&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=Regulation%20of%20Myosin%20Phosphatase%20by%20Rho%20and%20Rho-Associated%20Kinase%20(Rho-%20Kinase)&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Kimura,%20Kazushi&rft.date=1996-07-12&rft.volume=273&rft.issue=5272&rft.spage=245&rft.epage=248&rft.pages=245-248&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.273.5272.245&rft_dat=%3Cgale_proqu%3EA18500966%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213562624&rft_id=info:pmid/8662509&rft_galeid=A18500966&rft_jstor_id=2890422&rfr_iscdi=true |