p190RhoGAP is the convergence point of adhesion signals from α_5β_1 integrin and syndecan-4

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p190RhoGAP is the convergence point of adhesion signals from α_5β_1 integrin and syndecan-4

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dc.contributor.author Bass, Mark D.
dc.contributor.author Morgan, Mark R.
dc.contributor.author Roach, Kirsty A.
dc.contributor.author Settleman, Jeffrey Evan
dc.contributor.author Goryachev, Andrew B.
dc.contributor.author Humphries, Martin J.
dc.date.accessioned 2011-03-04T16:43:01Z
dc.date.issued 2008
dc.identifier.citation Bass, Mark D., Mark R. Morgan, Kirsty A. Roach, Jeffrey Settleman, Andrew B. Goryachev, and Martin J. Humphries. 2008. p190RhoGAP is the convergence point of adhesion signals from α_5β_1 integrin and syndecan-4. The Journal of Cell Biology 181(6): 1013-1026. en_US
dc.identifier.issn 0021-9525 en_US
dc.identifier.uri http://nrs.harvard.edu/urn-3:HUL.InstRepos:4737468
dc.description.abstract The fibronectin receptors α_5β_1 integrin and syndecan-4 cocluster in focal adhesions and coordinate cell migration by making individual contributions to the suppression of RhoA activity during matrix engagement. p190Rho–guanosine triphosphatase–activating protein (GAP) is known to inhibit RhoA during the early stages of cell spreading in an Src-dependent manner. This paper dissects the mechanisms of p190RhoGAP regulation and distinguishes the contributions of α_5β_1 integrin and syndecan-4. Matrix-induced tyrosine phosphorylation of p190RhoGAP is stimulated solely by engagement of α_5β_1 integrin and is independent of syndecan-4. Parallel engagement of syndecan-4 causes redistribution of the tyrosine-phosphorylated pool of p190RhoGAP between membrane and cytosolic fractions by a mechanism that requires direct activation of protein kinase C α by syndecan-4. Activation of both pathways is necessary for the efficient regulation of RhoA and, as a consequence, focal adhesion formation. Accordingly, we identify p190RhoGAP as the convergence point for adhesive signals mediated by α_5β_1 integrin and syndecan-4. This molecular mechanism explains the cooperation between extracellular matrix receptors during cell adhesion. en_US
dc.language.iso en_US en_US
dc.publisher The Rockefeller University Press en_US
dc.relation.isversionof doi:10.1083/jcb.200711129 en_US
dc.relation.hasversion http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2426943/pdf/ en_US
dash.license LAA
dc.subject Cell-Adhesion en_US
dc.subject Directional Migration en_US
dc.subject Cytoplasmic Domain en_US
dc.subject Binding Domain en_US
dc.subject RhoA Activity en_US
dc.subject Wound Repair en_US
dc.subject SRC Kinase en_US
dc.subject PKC-Alpha en_US
dc.subject C-SRC en_US
dc.subject Fibronectin en_US
dc.title p190RhoGAP is the convergence point of adhesion signals from α_5β_1 integrin and syndecan-4 en_US
dc.type Journal Article en_US
dc.description.version Version of Record en_US
dc.relation.journal The Journal of Cell Biology en_US
dash.depositing.author Settleman, Jeffrey Evan
dc.date.available 2011-03-04T16:43:01Z
dash.affiliation.other HMS^Medicine-Massachusetts General Hospital en_US

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