Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase A

被引：40

作者：

Hepp, R ^{[1
]}

Cabaniols, JP ^{[1
]}

Roche, PA ^{[1
]}

机构：

[1] NCI, Expt Immunol Branch, NIH, Bethesda, MD 20892 USA

来源：

FEBS LETTERS | 2002年 / 532卷 / 1-2期

关键词：

SNAP receptor; synaptosome-associated protein of 25 kDa; exocytosis; phosphorylation;

D O I：

10.1016/S0014-5793(02)03629-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

SNAP-25 is a key protein required for the fusion of synaptic vesicles with the plasma membrane during exocytosis. This study establishes that SNAP-25 is differentially phosphorylated by protein kinase C and protein kinase A in neuroendocrine PC12 cells. Using phosphopeptide mapping and site-directed mutagenesis we identified both Thr138 and Ser187 as the targets of SNAP-25 phosphorylation by protein kinase C and Thr138 as the exclusive site of SNAP-25 phosphorylation by protein kinase A in vivo. Finally, despite published data to the contrary, we demonstrate that stimulation of regulated exocytosis under physiological conditions is independent of a measurable increase in SNAP-25 phosphorylation in PC12 cells. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：52 / 56

页数：5

共 17 条

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