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. 1992 Dec 15;89(24):11983–11987. doi: 10.1073/pnas.89.24.11983

Odor-induced phosphorylation of olfactory cilia proteins.

I Boekhoff 1, S Schleicher 1, J Strotmann 1, H Breer 1
PMCID: PMC50682  PMID: 1334554

Abstract

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.

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Selected References

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