Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro

Reiko Minakami, Nobuyoshi Jinnai, Hiroyuki Sugiyama

Research output: Contribution to journalArticle

118 Citations (Scopus)

Abstract

Metabotropic glutamate receptors, which are members of a G protein- coupled receptor family, mediate the glutamate responses by coupling to the intracellular signal transduction pathway. We herein report that calmodulin (CaM) interacts with the metabotropic glutamate receptor subtype 5 (mGluR5) in a Ca2+-dependent manner in vitro. CaM is capable of binding on two distinct sites in the COOH-terminal intracellular region of the receptor with different affinities. The CaM binding domains are separated by an alternatively spliced exon cassette present in one of the splicing isoforms of mGluR5. By using fusion proteins and synthetic peptides we showed that protein kinase C phosphorylates both CaM binding regions. This phosphorylation is inhibited by the binding of CaM to the receptor, and conversely the binding is inhibited by the phosphorylation. These antagonisms of the CaM binding and phosphorylation thus suggest the possibility that they regulate the receptor responses in vivo.

Original languageEnglish
Pages (from-to)20291-20298
Number of pages8
JournalJournal of Biological Chemistry
Volume272
Issue number32
DOIs
Publication statusPublished - Aug 8 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro'. Together they form a unique fingerprint.

  • Cite this