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dc.contributor.author Lévay, Magdolna
dc.contributor.author Bartos, Balázs Ádám
dc.contributor.author Ligeti, Erzsébet
dc.date.accessioned 2016-09-13T09:14:53Z
dc.date.available 2016-09-13T09:14:53Z
dc.date.issued 2013
dc.identifier 84876337880
dc.identifier.citation pagination=1388-1394; journalVolume=25; journalIssueNumber=6; journalTitle=CELLULAR SIGNALLING;
dc.identifier.uri http://repo.lib.semmelweis.hu//handle/123456789/2678
dc.identifier.uri doi:10.1016/j.cellsig.2013.03.004
dc.description.abstract p190RhoGAP is a GTPase-activating protein (GAP) known to regulate actin cytoskeleton dynamics by decreasing RhoGTP levels through activation of the intrinsic GTPase activity of Rho. Although the GAP domain of p190RhoGAP stimulates the intrinsic' GTPase activity of several Rho family members (Rho, Rac, Cdc42) under in vitro conditions, p190RhoGAP is generally regarded as a GAP for RhoA in the cell. The cellular RacGAP activity of the protein has not been proven directly. We have previously shown that the in vitro RacGAP and RhoGAP activity of p190RhoGAP was inversely regulated through a polybasic region of the protein. Here we provide evidence that p190RhoGAP shows remarkable GAP activity toward Rac also in the cell. The cellular RacGAP activity of p190RhoGAP requires an intact polybasic region adjacent to the GAP domain whereas the RhoGAP activity is inhibited by the same domain. Our data indicate that through its alternating RacGAP and RhoGAP activity, p190RhoGAP plays a more complex role in the Rac-Rho antagonism than it was realized earlier. © 2013 Elsevier Inc.
dc.relation.ispartof urn:issn:0898-6568
dc.title P190RhoGAP has cellular RacGAP activity regulated by a polybasic region
dc.type Journal Article
dc.date.updated 2015-11-24T16:12:03Z
dc.language.rfc3066 en
dc.identifier.mtmt 2318092
dc.identifier.wos 000319176000006
dc.identifier.pubmed 23499677
dc.contributor.department SE/AOK/I/Élettani Intézet
dc.contributor.institution Semmelweis Egyetem


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