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- W2022102563 abstract "Metabotropic glutamate receptors (mGluRs) coupled to phosphoinositide hydrolysis desensitize in response to prolonged or repeated agonist exposure, and evidence suggests that this involves activation of protein kinase C (PKC). The present studies were undertaken to determine if cloned mGluR5 undergoes similar PKC-mediated desensitization and to investigate the molecular mechanism underlying PKC-induced desensitization. In Xenopus oocytes, both mGluR5a and mGluR5b showed pronounced desensitization in response to a brief activation by glutamate. Pharmacological studies clearly suggest that this desensitization requires PKC-mediated phosphorylation. Analysis of PKC consensus phosphorylation site mutants suggests that PKC phosphorylates mGluR5 at multiple sites to induce a relatively rapid form of desensitization. Because mGluRs play important roles in synaptic plasticity and in excitotoxicity, this desensitization may be involved in the dynamic regulation of these processes." @default.
- W2022102563 created "2016-06-24" @default.
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- W2022102563 date "1998-01-01" @default.
- W2022102563 modified "2023-10-03" @default.
- W2022102563 title "Role of Protein Kinase C Phosphorylation in Rapid Desensitization of Metabotropic Glutamate Receptor 5" @default.
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- W2022102563 doi "https://doi.org/10.1016/s0896-6273(00)80442-0" @default.
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