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Rapid agonist mediated phosphorylation of the metabotropic glutamate receptor 1α by protein kinase C in permanently transfected BHK cells
Author(s) -
Alaluf Simon,
Mulvihill Eileen R.,
McIlhinney Robert A.J.
Publication year - 1995
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 - 10.1016/0014-5793(95)00575-t
Subject(s) - metabotropic glutamate receptor 6 , metabotropic glutamate receptor 1 , metabotropic glutamate receptor , metabotropic glutamate receptor 2 , metabotropic glutamate receptor 7 , chemistry , metabotropic glutamate receptor 5 , metabotropic glutamate receptor 4 , agonist , phosphorylation , transfection , metabotropic glutamate receptor 3 , microbiology and biotechnology , biochemistry , receptor , biology , gene
Clonal BHK cells permanently transfected with the metabotropic glutamate receptor 1α (mGluR1α), which is coupled to phospholipase C, were used to study the phosphorylation state of the receptor. Cells were labelled with 32 PO 4 3− , lysed, the receptor immunoprecipitated with specific anti‐peptide antibodies and the immunoprecipitates analysed by SDS‐PAGE followed by autoradiography. A significant basal level of receptor phosphorylation was observed which was rapidly and transiently increased in response to agonist activation of the receptor. This agonist effect was found to be dose dependent with a rapid time course and could be abolished by the specific PKC inhibitor Ro318220, suggesting that PKC was responsible for the agonist mediated phosphorylation of the receptor.