PI(3,4,5)P3 (PIP3) binds DAPP1 (BAM32) and DAPP1 is phosphorylated

Stable Identifier
Reaction [uncertain]
Homo sapiens
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DAPP1 (BAM32) is recruited to the plasma membrane by the binding of its PH domain to phosphoinositol 3,4,5-trisphosphate (PIP3) (Dowler et al. 1999, Marshall et al. 2000, Ferguson et al. 2000). DAPP1 also binds phosphatidylinositol 3,4-bisphosphate (Dowler et al. 1999, Ferguson et al. 2000) and therefore remains bound at the plasma membrane after PIP3 has been dephosphorylated by phosphatases. At the plasma membrane DAPP1 is phosphorylated by a Src family kinase, likely LYN in B cells (Dowler et al. 2000).
Literature References
PubMed ID Title Journal Year
10432293 DAPP1: a dual adaptor for phosphotyrosine and 3-phosphoinositides

Downes, CP, Currie, RA, Dowler, S, Alessi, DR

Biochem. J. 1999
10770799 A novel B lymphocyte-associated adaptor protein, Bam32, regulates antigen receptor signaling downstream of phosphatidylinositol 3-kinase

Thomas, S, Yun, TJ, Lerner, CG, Clark, EA, Marshall, AJ, Disteche, CM, Niiro, H

J Exp Med 2000
10983984 Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains

Kavran, JM, Fournier, E, Sankaran, VG, Isakoff, SJ, Lemmon, MA, Skolnik, EY, Ferguson, KM

Mol. Cell 2000
10880360 Phosphoinositide 3-kinase-dependent phosphorylation of the dual adaptor for phosphotyrosine and 3-phosphoinositides by the Src family of tyrosine kinase

Morrice, N, Montalvo, L, Dowler, S, Alessi, DR, Cantrell, D

Biochem. J. 2000
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