PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding

被引：38

作者：

Airas, JM ^{[1
]}

Betz, H ^{[1
]}

El Far, O ^{[1
]}

机构：

[1] Max Planck Inst Brain Res, Dept Neurochem, D-60528 Frankfurt, Germany

来源：

FEBS LETTERS | 2001年 / 494卷 / 1-2期

关键词：

metabotropic glutamate receptor; protein kinase C; calmodulin; phosphorylation;

D O I：

10.1016/S0014-5793(01)02311-0

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：

Group III metabotropic glutamate receptors (mGluRs) serve as presynaptic receptors that mediate feedback inhibition of glutamate release via a Ca2+/calmodulin (CaM)-dependent mechanism. In vitro phosphorylation of mGluR7A by protein kinase C (PKC) prevents its interaction with Ca2+/CaM. In addition, activation of PKC leads to an inhibition of mGluR signaling. Here, we demonstrate that disrupting CaM binding to mGluR7A by PKC in vitro is due to phosphorylation of a highly conserved serine residue, S862, We propose charge neutralization of the CaM binding consensus sequence resulting from phosphorylation to constitute a general mechanism for the regulation of presynaptic mGluR signaling. (C) 2001 Federation of European Biochemical Societies, Published by Elsevier Science B,V, All rights reserved.

引用

页码：60 / 63

页数：4

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