DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides

被引：123

作者：

Dowler, S ^{[1
]}

Currie, RA ^{[1
]}

Downes, CP ^{[1
]}

Alessi, DR ^{[1
]}

机构：

[1] Univ Dundee, Dept Biochem, MRC, Prot Phosphorylat Unit, Dundee DD1 5EH, Scotland

来源：

BIOCHEMICAL JOURNAL | 1999年 / 342卷

关键词：

DAPP; PI; 3-kinase; phosphoinositide; PH domain; SH2; domain;

D O I：

10.1042/0264-6021:3420007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have identified a novel 280 amino acid protein which contains a putative myristoylation site at its N-terminus followed by an Src homology (SH2) domain and a pleckstrin homology (PH) domain at its C-terminus. It has been termed dual adaptor for phosphotyrosine: and 3-phosphoinositides (DAPP1). DAPP1 is widely expressed and exhibits high-affinity interactions with PtdIns(3,4,5)P-3 and PtdIns(3,4)P-2, but not with other phospholipids tested. These observations predict that DAPP1 will interact with both tyrosine phosphorylated proteins and 3-phosphoinositides and may therefore play a role in regulating the location and/or activity of such proteins(s) in response to agonists that elevate PtdIns(3,4,5)P-3 and PtdIns(3,4)P-2.

引用

页码：7 / 12

页数：6

共 24 条

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