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Chem. Senses 24: 295-299, 1999
© Oxford University Press

Protein Kinase Cß and {delta} Selectively Phosphorylate Odorant and Metabotropic Glutamate Receptors

Kathryn F. Medler and Richard C. Bruch

Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA

Correspondence to be sent to: Richard C. Bruch, Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA. e-mail:rbruch{at}lsuvm.sncc.lsu.edu

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 Cß and {delta} phosphorylated an intracellular consensus phosphorylation site in the metabotropic glutamate receptor. Only protein kinase C {delta} phosphorylated a novel extracellular consensus phosphorylation site in the odorant receptor. These results suggest differential regulation of these receptors by protein kinase C isotypes.


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