Protein kinase Cbeta and delta selectively phosphorylate odorant and metabotropic glutamate receptors.
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.
Department of Biological Sciences, Louisiana State University, Baton Rouge 70803, USA.
K F
KF
Medler
R C
RC
Bruch
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002397:Catfishes; D007527:Isoenzymes / Q000737:chemistry*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010766:Phosphorylation; D011493:Protein Kinase C / Q000737:chemistry*; D064546:Protein Kinase C beta; D018094:Receptors, Metabotropic Glutamate / Q000737:chemistry*; D018035:Receptors, Odorant / Q000737:chemistry*
D007527:Isoenzymes; D018094:Receptors, Metabotropic Glutamate; D018035:Receptors, Odorant; C087857:protein kinase C gamma; D011493:Protein Kinase C; D064546:Protein Kinase C beta