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Two phosphorylation-independent sites on the p85 SH2 domains bind A-Raf kinase.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Fang Y,Johnson LM,Mahon ES,Anderson DH

doi

10.1006/bbrc.2002.6347

subject

Has Abstract

pub_date

2002-02-01 00:00:00

pages

1267-74

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006291X02963473

journal_volume

290

pub_type

杂志文章

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