Work

DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides

Year: 1999

Type: article

Abstract: 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).

Source: Biochemical Journal

DOI: 10.1042/0264-6021:3420007

Authors: Simon DOWLER, Richard A. CURRIE, C. Peter DOWNES, Dario R. ALESSI

Institutions: University of Dundee, MRC Protein Phosphorylation and Ubiquitylation Unit

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Directorate for Biological Sciences, Medical Research Council, Biotechnology and Biological Sciences Research Council

OpenAlex ID: W4239979702