Title : Phosphoinositide 3-kinase-dependent phosphorylation of the dual adaptor for phosphotyrosine and 3-phosphoinositides by the Src family of tyrosine kinase.

Pub. Date : 2000 Jul 15

PMID : 10880360






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 DAPP1 exhibits a high-affinity interaction with PtdIns(3,4,5)P(3) and PtdIns(3,4)P(2), which bind to the PH domain. phosphoinositide-3,4-bisphosphate dual adaptor of phosphotyrosine and 3-phosphoinositides 1 Homo sapiens
2 Treatment of cells with phosphoinositide 3-kinase (PI 3-kinase) inhibitors or expression of a dominant-negative PI 3-kinase prevent phosphorylation of DAPP1 at Tyr(139), and a PH-domain mutant of DAPP1, which does not interact with PtdIns(3,4,5)P(3) or PtdIns(3,4)P(2), is not phosphorylated at Tyr(139) following agonist stimulation of cells. phosphoinositide-3,4-bisphosphate dual adaptor of phosphotyrosine and 3-phosphoinositides 1 Homo sapiens
3 These findings indicate that, following activation of PI 3-kinases, PtdIns(3,4,5)P(3) or PtdIns(3,4)P(2) bind to DAPP1, recruiting it to the plasma membrane where it becomes phosphorylated at Tyr(139) by a Src-family tyrosine kinase. phosphoinositide-3,4-bisphosphate dual adaptor of phosphotyrosine and 3-phosphoinositides 1 Homo sapiens