PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding
PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding
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DOI：
10.1016/s0014-5793(01)02311-0
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发表时间：
2001-04-06
期刊：
影响因子：
3.5
通讯作者：
El Far, O
中科院分区：
文献类型：
--
作者：
Airas, JM;Betz, H;El Far, O
III组代谢型谷氨酸受体（mGluRs）作为突触前受体，通过Ca 2 +/钙调蛋白（CaM）依赖性机制介导谷氨酸释放的反馈抑制。蛋白激酶C（PKC）对mGluR 7A的体外磷酸化阻止其与Ca 2 +/CaM的相互作用。此外，PKC的活化导致mGluR信号传导的抑制。在这里，我们证明，破坏钙调素结合mGluR 7A的PKC在体外是由于磷酸化的高度保守的丝氨酸残基，S862，我们建议电荷中和的钙调素结合的共识序列导致磷酸化，构成一个一般的机制调节突触前mGluR信号。(C)2001年欧洲生物化学学会联合会，由Elsevier Science B，V出版，保留所有权利。
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.