Cyclic phosphorylation-dephosphorylation of rhodopsin in retina by protein kinase FA (the activator of ATP.Mg-dependent protein phosphatase).

Journal Article

The ATP.Mg-dependent protein phosphatase activating factor (protein kinase FA) was identified to exist in bovine retina. Furthermore, rhodopsin, the visual light pigment associated with rod outer segments in retina, could be well phosphorylated by kinase FA to about 0.9 mol of phosphates per mol of protein. Moreover, more than 90% of the phosphates in [32P]-rhodopsin could be completely removed by ATP.Mg-dependent protein phosphatase and the rhodopsin phosphatase activity was strictly kinase FA-dependent. Taken together, the results provide initial evidence that a cyclic phosphorylation-dephosphorylation of rhodopsin can be controlled by the retina-associated protein kinase FA, representing an efficient cyclic cascade mechanism possibly involved in the rapid regulation of rhodopsin function in retina.

Full Text

Duke Authors

Cited Authors

  • Yang, SD; Benovic, JL; Fong, YL; Caron, MG; Lefkowitz, RJ

Published Date

  • August 15, 1991

Published In

Volume / Issue

  • 178 / 3

Start / End Page

  • 1306 - 1311

PubMed ID

  • 1651717

International Standard Serial Number (ISSN)

  • 0006-291X

Language

  • eng

Conference Location

  • United States