Protein kinase Cbeta and delta selectively phosphorylate odorant and metabotropic glutamate receptors

Chem Senses. 1999 Jun;24(3):295-9. doi: 10.1093/chemse/24.3.295.

Abstract

Recombinant protein segments from a metabotropic glutamate receptor and from an odorant receptor were used as substrates in protein kinase C phosphorylation assays. Protein kinase Cbeta and delta phosphorylated an intracellular consensus phosphorylation site in the metabotropic glutamate receptor. Only protein kinase Cdelta phosphorylated a novel extracellular consensus phosphorylation site in the odorant receptor. These results suggest differential regulation of these receptors by protein kinase C isotypes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Catfishes
  • Isoenzymes / chemistry*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Protein Kinase C / chemistry*
  • Protein Kinase C beta
  • Receptors, Metabotropic Glutamate / chemistry*
  • Receptors, Odorant / chemistry*

Substances

  • Isoenzymes
  • Receptors, Metabotropic Glutamate
  • Receptors, Odorant
  • protein kinase C gamma
  • Protein Kinase C
  • Protein Kinase C beta