Biochemical Journal · 1999 · 97 citations · 0 references
Life SciencesBiochemistryMolecular BiologyCell SignalingProtein BiochemistrySignal TransductionAdaptor ProteinsMembrane ReceptorsProtein Kinase CascadesProtein PhosphorylationProtein-lipid InteractionsSignal Transduction ComplexesPhosphatidylinositol 3, 4, 5-Trisphosphate SignalingPhosphatidylinositol 4, 5-BisphosphatePhosphoinositide BindingPhosphoinositide KinasesPhosphoinositide PhosphorylationPhosphoinositide-binding DomainsPhosphotyrosine Binding DomainsPleckstrin Homology Domains
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.