SPIN90-IRSp53 complex participates in Rac-induced membrane ruffling

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dc.contributor.authorTeodorof C.ko
dc.contributor.authorBae J.I.ko
dc.contributor.authorKim S.-M.ko
dc.contributor.authorOh H.J.ko
dc.contributor.authorKang Y.S.ko
dc.contributor.authorChoi J.ko
dc.contributor.authorChun J.-S.ko
dc.contributor.authorSong W.K.ko
dc.date.accessioned2013-03-08T23:38:49Z-
dc.date.available2013-03-08T23:38:49Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2009-
dc.identifier.citationEXPERIMENTAL CELL RESEARCH, v.315, no.14, pp.2410 - 2419-
dc.identifier.issn0014-4827-
dc.identifier.urihttp://hdl.handle.net/10203/94680-
dc.description.abstractSPIN90 is a key regulator of actin cytoskeletal organization. Using the BioGRID(beta) database (General Repository for Interaction Datasets), we identified IRSp53 as a binding partner of SPIN90, and confirmed the in vivo formation of a SPIN90-IRSp53 complex mediated through direct association of the proline-rich domain (PRD) of SPIN90 with the SH3 domain of IRSp53. SPIN90 and IRSp53 positively cooperated to mediate Rac activation, and co-expression of SPIN90 and IRSp53 in COS-7 cells led to the complex formation of SPIN90-IRSp53 in the leading edge of cells. PDGF treatment induced strong colocalization of SPIN90 and IRSp53 at membrane protrusions. Within such PDGF-induced protrusions, knockdown of SPIN90 protein using siRNA significantly reduced lamellipodia-like protrusions as well as localization of IRSp53 at those sites. Finally, competitive inhibition of SPIN90-IRSp53 binding by SPIN90 PRD dramatically reduced ruffle formation, further suggesting that SPIN90 plays a key role in the formation of the membrane protrusions associated with cell motility. (C) 2009 Elsevier Inc. All rights reserved.-
dc.languageEnglish-
dc.publisherELSEVIER INC-
dc.subjectINSULIN-RECEPTOR SUBSTRATE-
dc.subjectMDIA-INTERACTING PROTEIN-
dc.subjectACTIN STRESS FIBERS-
dc.subjectBINDING-PROTEIN-
dc.subjectN-WASP-
dc.subjectIRSP53-
dc.subjectCDC42-
dc.subjectFILOPODIA-
dc.subjectRHO-
dc.subjectACTIVATION-
dc.titleSPIN90-IRSp53 complex participates in Rac-induced membrane ruffling-
dc.typeArticle-
dc.identifier.wosid000267813000007-
dc.identifier.scopusid2-s2.0-67649197339-
dc.type.rimsART-
dc.citation.volume315-
dc.citation.issue14-
dc.citation.beginningpage2410-
dc.citation.endingpage2419-
dc.citation.publicationnameEXPERIMENTAL CELL RESEARCH-
dc.identifier.doi10.1016/j.yexcr.2009.05.010-
dc.contributor.localauthorChoi J.-
dc.contributor.nonIdAuthorTeodorof C.-
dc.contributor.nonIdAuthorBae J.I.-
dc.contributor.nonIdAuthorKim S.-M.-
dc.contributor.nonIdAuthorOh H.J.-
dc.contributor.nonIdAuthorKang Y.S.-
dc.contributor.nonIdAuthorChun J.-S.-
dc.contributor.nonIdAuthorSong W.K.-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorSPIN90-
dc.subject.keywordAuthorIRSp53-
dc.subject.keywordAuthorRac1-
dc.subject.keywordAuthorCytoskeleton-
dc.subject.keywordAuthorMembrane ruffling-
dc.subject.keywordAuthorActin-
dc.subject.keywordPlusINSULIN-RECEPTOR SUBSTRATE-
dc.subject.keywordPlusMDIA-INTERACTING PROTEIN-
dc.subject.keywordPlusACTIN STRESS FIBERS-
dc.subject.keywordPlusBINDING-PROTEIN-
dc.subject.keywordPlusN-WASP-
dc.subject.keywordPlusIRSP53-
dc.subject.keywordPlusCDC42-
dc.subject.keywordPlusFILOPODIA-
dc.subject.keywordPlusRHO-
dc.subject.keywordPlusACTIVATION-
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