Odor-induced phosphorylation of olfactory cilia proteins.
Stimulation of isolated rat olfactory cilia in the presence of [gamma-32P]ATP leads to a significantly enhanced incorporation of [32P]phosphate. Depending on the type of odorants applied, the induced phosphorylation is completely blocked by specific inhibitors of either protein kinase A or protein kinase C. Time-course experiments indicate that the odor-induced modification of ciliary proteins is transient; the intensity of labeling decayed over time (1-10 sec). Separation of ciliary proteins by SDS/polyacrylamide gel electrophoresis followed by autoradiography demonstrated that upon stimulation with lilial, a single polypeptide (50,000 Da) was phosphorylated; the size of the modified protein is in line with the hypothesis that odorant receptors are phosphorylated subsequent to activation by specific odors.
Boekhoff
I
I
University Stuttgart-Hohenheim, Institute of Zoophysiology, Federal Republic of Germany.
Schleicher
S
S
Strotmann
J
J
Breer
H
H
D000818:Animals; D002923:Cilia / Q000378:metabolism; D000242:Cyclic AMP / Q000502:physiology; D015544:Inositol 1,4,5-Trisphosphate / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009831:Olfactory Mucosa / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000502:physiology; D011494:Protein Kinases / Q000502:physiology; D051381:Rats; D017207:Rats, Sprague-Dawley; D015290:Second Messenger Systems; D011984:Sensory Receptor Cells / Q000378:metabolism; D012903:Smell / Q000502:physiology*
D009419:Nerve Tissue Proteins; D015544:Inositol 1,4,5-Trisphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D011493:Protein Kinase C