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)P3 and PtdIns(3,4)P2, 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)P3 and PtdIns(3,4)P2.
Research Article| August 10 1999
DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides
Simon DOWLER 1
*MRC Protein Phosphorylation Unit, Department of Biochemistry, MSI/WTB Complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
1To whom correspondence should be addressed (e-mail email@example.com).
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Richard A. CURRIE;
C. Peter DOWNES;
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Simon DOWLER, Richard A. CURRIE, C. Peter DOWNES, Dario R. ALESSI; DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides. Biochem J 15 August 1999; 342 (1): 7–12. doi: https://doi.org/10.1042/bj3420007
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