Substrate specificity: PI(3)Kγ has it both ways

Jonathan M. Backer

doi:10.1038/ncb0805-773

Substrate specificity: PI(3)Kγ has it both ways

Jonathan M. Backer

Molecular Pharmacology

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Phosphoinositide 3-kinases (PI(3)Ks) are mainly known for their lipid kinase activity in various cellular functions; however, PI(3)Ks also have protein kinase activity. Non-muscle tropomyosin has been identified as a novel protein target for PI(3)Kγ. Phosphorylation of tropomyosin is required for β-adrenergic receptor internalization, providing new insight into PI(3)K function during clathrin-mediated endocytosis.

Original language	English (US)
Pages (from-to)	773-774
Number of pages	2
Journal	Nature Cell Biology
Volume	7
Issue number	8
DOIs	https://doi.org/10.1038/ncb0805-773
State	Published - Aug 2005

ASJC Scopus subject areas

Cell Biology

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abstract = "Phosphoinositide 3-kinases (PI(3)Ks) are mainly known for their lipid kinase activity in various cellular functions; however, PI(3)Ks also have protein kinase activity. Non-muscle tropomyosin has been identified as a novel protein target for PI(3)Kγ. Phosphorylation of tropomyosin is required for β-adrenergic receptor internalization, providing new insight into PI(3)K function during clathrin-mediated endocytosis.",

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Substrate specificity: PI(3)Kγ has it both ways

Abstract

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