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• W1964316904 endingPage "1274" @default.
• W1964316904 startingPage "1267" @default.
• W1964316904 abstract "Src homology 2 (SH2) domains mediate phosphotyrosine (pY)-dependent protein:protein interactions involved in signal transduction pathways. We have found that the SH2 domains of the 85-kDa alpha subunit (p85) of phosphatidylinositol 3-kinase (PI3 kinase) bind directly to the serine/threonine kinase A-Raf. In this report we show that the p85 SH2:A-Raf interaction is phosphorylation-independent. The affinity of the p85 C-SH2 domain for A-Raf and phosphopeptide pY751 was similar, raising the possibility that a p85:A-Raf complex may play a role in the coordinated regulation of the PI3 kinase and Raf-MAP kinase pathways. We further show that the p85 C-SH2 domain contains two distinct binding sites for A-Raf; one overlapping the phosphotyrosine-dependent binding site and the other a separate phosphorylation-independent site. This is the first evidence for a second binding site on an SH2 domain, distinct from the phosphotyrosine-binding pocket." @default.
• W1964316904 created "2016-06-24" @default.
• W1964316904 creator A5026094081 @default.
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• W1964316904 date "2002-02-01" @default.
• W1964316904 modified "2023-10-17" @default.
• W1964316904 title "Two Phosphorylation-Independent Sites on the p85 SH2 Domains Bind A-Raf Kinase" @default.
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• W1964316904 doi "https://doi.org/10.1006/bbrc.2002.6347" @default.
• W1964316904 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11812000" @default.
• W1964316904 hasPublicationYear "2002" @default.
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