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
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
收藏
页码:7 / 12
页数:6
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