Publications | DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides

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).

Principal Investigator(s):

Author(s):
Dowler, S., Currie, R. A., Downes, C. P., Alessi, D. R.

PubMed:
10432293
Citation:
Dowler, S., Currie, R. A., Downes, C. P., Alessi, D. R.
Biochem J
1999
342
7-12
PMID: 10432293