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

Senin, Ivan I.¹  Zargarov, Aminullah A.²  Philippov, Pavel P.¹  Akhtar, Muhammad³ 

[1] Department of Enzymology, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia;Branch of Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Puschino, Moscow Region 142292, Russia;Department of Biochemistry, University of Southampton, Basset Crescent East, Southampton, UK S09 3TU

关键词: Photoreception;    Phosphorylation;    Rhodopsin;    Rhodopsin kinase;    Recoverin;    Calcium-binding protein;    Retinal rod cell;    Rho;    unbleached rhodopsin;    Rho*;    bleached rhodopsin;    Rho-P;    phosphorylated unbleached rhodopsin;    Rho*-P;    phosphorylated bleached rhodopsin;    RK;    non-activated rhodopsin kinase;    RK*;    activated rhodopsin kinase;    ROS;    rod outer segment;    [Ca2+]f;    free Ca2+ concentration;   

DOI  :  10.1016/S0014-5793(97)00434-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown