DC Field | Value | Language |
---|---|---|
dc.contributor.author | Teodorof C. | ko |
dc.contributor.author | Bae J.I. | ko |
dc.contributor.author | Kim S.-M. | ko |
dc.contributor.author | Oh H.J. | ko |
dc.contributor.author | Kang Y.S. | ko |
dc.contributor.author | Choi J. | ko |
dc.contributor.author | Chun J.-S. | ko |
dc.contributor.author | Song W.K. | ko |
dc.date.accessioned | 2013-03-08T23:38:49Z | - |
dc.date.available | 2013-03-08T23:38:49Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | EXPERIMENTAL CELL RESEARCH, v.315, no.14, pp.2410 - 2419 | - |
dc.identifier.issn | 0014-4827 | - |
dc.identifier.uri | http://hdl.handle.net/10203/94680 | - |
dc.description.abstract | SPIN90 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.language | English | - |
dc.publisher | ELSEVIER INC | - |
dc.subject | INSULIN-RECEPTOR SUBSTRATE | - |
dc.subject | MDIA-INTERACTING PROTEIN | - |
dc.subject | ACTIN STRESS FIBERS | - |
dc.subject | BINDING-PROTEIN | - |
dc.subject | N-WASP | - |
dc.subject | IRSP53 | - |
dc.subject | CDC42 | - |
dc.subject | FILOPODIA | - |
dc.subject | RHO | - |
dc.subject | ACTIVATION | - |
dc.title | SPIN90-IRSp53 complex participates in Rac-induced membrane ruffling | - |
dc.type | Article | - |
dc.identifier.wosid | 000267813000007 | - |
dc.identifier.scopusid | 2-s2.0-67649197339 | - |
dc.type.rims | ART | - |
dc.citation.volume | 315 | - |
dc.citation.issue | 14 | - |
dc.citation.beginningpage | 2410 | - |
dc.citation.endingpage | 2419 | - |
dc.citation.publicationname | EXPERIMENTAL CELL RESEARCH | - |
dc.identifier.doi | 10.1016/j.yexcr.2009.05.010 | - |
dc.contributor.localauthor | Choi J. | - |
dc.contributor.nonIdAuthor | Teodorof C. | - |
dc.contributor.nonIdAuthor | Bae J.I. | - |
dc.contributor.nonIdAuthor | Kim S.-M. | - |
dc.contributor.nonIdAuthor | Oh H.J. | - |
dc.contributor.nonIdAuthor | Kang Y.S. | - |
dc.contributor.nonIdAuthor | Chun J.-S. | - |
dc.contributor.nonIdAuthor | Song W.K. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | SPIN90 | - |
dc.subject.keywordAuthor | IRSp53 | - |
dc.subject.keywordAuthor | Rac1 | - |
dc.subject.keywordAuthor | Cytoskeleton | - |
dc.subject.keywordAuthor | Membrane ruffling | - |
dc.subject.keywordAuthor | Actin | - |
dc.subject.keywordPlus | INSULIN-RECEPTOR SUBSTRATE | - |
dc.subject.keywordPlus | MDIA-INTERACTING PROTEIN | - |
dc.subject.keywordPlus | ACTIN STRESS FIBERS | - |
dc.subject.keywordPlus | BINDING-PROTEIN | - |
dc.subject.keywordPlus | N-WASP | - |
dc.subject.keywordPlus | IRSP53 | - |
dc.subject.keywordPlus | CDC42 | - |
dc.subject.keywordPlus | FILOPODIA | - |
dc.subject.keywordPlus | RHO | - |
dc.subject.keywordPlus | ACTIVATION | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.