Rhodopsin phosphorylation in bovine rod outer segments is more sensitive to the inhibitory action of recoverin at the low rhodopsin bleaching than it is at the high bleaching

FEBS Letters
I I SeninP P Philippov

Abstract

Recoverin, a calcium-binding protein, is supposed to have rhodopsin kinase as a target in the retinal rod cell. In the present work, we show that efficiency of recoverin as an inhibitor of rhodopsin phosphorylation in bovine rod outer segments is inversely proportional to the level of rhodopsin bleaching. These results, together with the data obtained previously in a reconstituted system (Senin et al. (1997) Biochem. J. 321, 551-555), allow us to hypothesize that recoverin might be responsible for a Ca2(+)-dependent regulation of the kinase in vivo, preventing it from participating in the phosphorylation of unbleached rhodopsin.

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Citations

Mar 31, 2000·Journal of Neuroscience Research·W CaoJ F McGinnis
Jul 9, 1998·Neuroscience Letters·N Dalil-ThineyC Versaux-Botteri
May 14, 2003·Progress in Retinal and Eye Research·Tadao MaedaKrzysztof Palczewski
Dec 15, 2000·The Biochemical Journal·R D Burgoyne, J L Weiss
Aug 25, 2001·Annual Review of Neuroscience·M E Burns, D A Baylor
Jan 31, 2006·Cancer Immunology, Immunotherapy : CII·Alexandr V BazhinStefan B Eichmüller
Aug 1, 2012·Cellular Signalling·Mikhail A KutuzovNelly Bennett
Dec 8, 2000·Biochimica Et Biophysica Acta·M SalleseA De Blasi
Jan 5, 1999·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·L IacovelliA de Blasi
Jul 17, 1998·Vision Research·J B HurleyG A Niemi

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