DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Seyun | ko |
dc.contributor.author | Lee, Seung-Hye | ko |
dc.contributor.author | Park, Dongeun | ko |
dc.date.accessioned | 2013-03-04T19:44:05Z | - |
dc.date.available | 2013-03-04T19:44:05Z | - |
dc.date.created | 2012-03-19 | - |
dc.date.created | 2012-03-19 | - |
dc.date.issued | 2001-04 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.276, no.14, pp.10581 - 10584 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/83877 | - |
dc.description.abstract | Pix, a p21-activated kinase-interacting exchange factor, is known to be involved in the regulation of Cdc42/ Pac GTPases, The 85-kDa beta Pix-a protein contains an Src homology 3 domain, the tandem Dbl homology and Pleckstrin homology domains, a proline-rich region, and a GIT1-binding domain. In addition to those domains, beta Pix-a also contains a putative leucine zipper domain at the C-terminal end. In this study, we demonstrate that the previously identified putative leucine zipper domain mediates the formation of beta Pix-a homodimers. Using in vittro and in vivo methodologies, we show that deletion of the leucine zipper domain is sufficient to abolish beta Pix-a homodimerization. In NIH3T3 fibroblast cells, expression of wild type beta Pix-a induces the formation of membrane ruffles. However, cells expressing the leucine zipper domain deletion mutant could not form membrane ruffle structures. Moreover, platelet derived growth factor-mediated cytoskeletal changes were completely blocked by the leucine zipper domain deletion mutant. The results suggest that the leucine zipper domain enables beta Pix-a to homodimerize, and homodimerization is essential for beta Pix-a signaling functions leading to the cytoskeletal reorganization. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | NUCLEOTIDE EXCHANGE FACTOR | - |
dc.subject | ACTIN STRESS FIBERS | - |
dc.subject | RHO GTPASES | - |
dc.subject | PROTEIN | - |
dc.subject | DOMAIN | - |
dc.subject | PAK | - |
dc.subject | RAC | - |
dc.subject | CLONING | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | TRANSFORMATION | - |
dc.title | Leucine zipper-mediated homodimerization of the p21-activated kinase-interacting factor, beta Pix - Implication for a role in cytoskeletal reorganization | - |
dc.type | Article | - |
dc.identifier.wosid | 000167980900002 | - |
dc.identifier.scopusid | 2-s2.0-0035815617 | - |
dc.type.rims | ART | - |
dc.citation.volume | 276 | - |
dc.citation.issue | 14 | - |
dc.citation.beginningpage | 10581 | - |
dc.citation.endingpage | 10584 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.identifier.doi | 10.1074/jbc.C000806200 | - |
dc.contributor.localauthor | Kim, Seyun | - |
dc.contributor.nonIdAuthor | Lee, Seung-Hye | - |
dc.contributor.nonIdAuthor | Park, Dongeun | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | NUCLEOTIDE EXCHANGE FACTOR | - |
dc.subject.keywordPlus | ACTIN STRESS FIBERS | - |
dc.subject.keywordPlus | RHO GTPASES | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | PAK | - |
dc.subject.keywordPlus | RAC | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | TRANSFORMATION | - |
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