Rhodopsin is the major in situ substrate of protein kinase C in rod outer segments of photoreceptors.


Phorbol ester treatment of 32P-labeled retinas results in a light-dependent alteration in the phosphorylation state of rhodopsin. Previously we reported that phorbol myristate acetate causes an increase in the phosphorylation state of rhodopsin in retinas exposed to a brief flash of light, with the greatest increase in phosphorylation observed at lower… (More)


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