DC Field | Value | Language |
---|---|---|
dc.contributor.author | Williams, JG | ko |
dc.contributor.author | Drugan, JK | ko |
dc.contributor.author | Yi, Gwan-Su | ko |
dc.contributor.author | Clark, GJ | ko |
dc.contributor.author | Der, CJ | ko |
dc.contributor.author | Campbell, SL | ko |
dc.date.accessioned | 2013-03-02T13:59:31Z | - |
dc.date.available | 2013-03-02T13:59:31Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-07 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.275, no.29, pp.22172 - 22179 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/73863 | - |
dc.description.abstract | Raf-1 is a critical downstream target of Ras and contains two distinct domains that bind Ras. The first Ras-binding site (RBS1) in Raf-1 has been shown to be essential for Ras-mediated translocation of Raf-1 to the plasma membrane, whereas the second site, in the Raf-1 cysteine rich domain (Raf-CRD), has been implicated in regulating Raf kinase activity. While recognition elements that promote Ras RBS1 complex formation have been characterized, relatively little is known about Ras/Raf-CRD interactions. In this study, we have characterized interactions important for Ras binding to the Raf-CRB. Reconciling conflicting reports, we found that these interactions are essentially independent of the guanine nucleotide bound state, but instead, are enhanced by post-translational modification of Ras. Specifically, our findings indicate that Res farnesylation is sufficient for stable association of Ras with the Raf-CRD. Furthermore, we have also identified a Raf-CRD variant that is impaired specifically in its interactions with Ras. MMR data also suggests that residues proximal to this mutation site on the Raf-CRD form contacts with Res. This Raf-CRD mutant impairs the ability of Ras to activate Raf kinase, thereby providing additional support that Ras interactions with the Raf-CRD are important for Ras-mediated activation of Raf-1. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | PROTEIN-KINASE-C | - |
dc.subject | RAF ZINC-FINGER | - |
dc.subject | PLASMA-MEMBRANE | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | CONTAINS ZINC | - |
dc.subject | HA-RAS | - |
dc.subject | ACTIVATION | - |
dc.subject | IDENTIFICATION | - |
dc.subject | RESIDUES | - |
dc.subject | TRANSFORMATION | - |
dc.title | Elucidation of binding determinants and functional consequences of Ras/Raf-cysteine-rich domain interactions | - |
dc.type | Article | - |
dc.identifier.wosid | 000088363800059 | - |
dc.identifier.scopusid | 2-s2.0-0034698068 | - |
dc.type.rims | ART | - |
dc.citation.volume | 275 | - |
dc.citation.issue | 29 | - |
dc.citation.beginningpage | 22172 | - |
dc.citation.endingpage | 22179 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.identifier.doi | 10.1074/jbc.M000397200 | - |
dc.contributor.localauthor | Yi, Gwan-Su | - |
dc.contributor.nonIdAuthor | Williams, JG | - |
dc.contributor.nonIdAuthor | Drugan, JK | - |
dc.contributor.nonIdAuthor | Clark, GJ | - |
dc.contributor.nonIdAuthor | Der, CJ | - |
dc.contributor.nonIdAuthor | Campbell, SL | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | PROTEIN-KINASE-C | - |
dc.subject.keywordPlus | RAF ZINC-FINGER | - |
dc.subject.keywordPlus | PLASMA-MEMBRANE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | CONTAINS ZINC | - |
dc.subject.keywordPlus | HA-RAS | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | RESIDUES | - |
dc.subject.keywordPlus | TRANSFORMATION | - |
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