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PKC phosphorylation of a conserved serine residue in the C‐terminus of group III metabotropic glutamate receptors inhibits calmodulin binding
Author(s) -
Airas José M,
Betz Heinrich,
El Far Oussama
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02311-0
Subject(s) - metabotropic glutamate receptor , class c gpcr , phosphorylation , protein kinase c , metabotropic glutamate receptor 7 , metabotropic glutamate receptor 5 , calmodulin , metabotropic receptor , metabotropic glutamate receptor 1 , serine , microbiology and biotechnology , metabotropic glutamate receptor 6 , metabotropic glutamate receptor 2 , glutamate receptor , biochemistry , chemistry , receptor , biology , enzyme
Group III metabotropic glutamate receptors (mGluRs) serve as presynaptic receptors that mediate feedback inhibition of glutamate release via a Ca 2+ /calmodulin (CaM)‐dependent mechanism. In vitro phosphorylation of mGluR7A by protein kinase C (PKC) prevents its interaction with Ca 2+ /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.