Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin

FEBS Letters

Arendt, Anatol¹  Puig, Jaime¹  Miller, Ron¹  Abdulaeva, Galina¹  Hargrave, Paul A.¹  Tomson, Farol L.¹  Hugh McDowell, J.¹ 

[1]Department of Ophthalmology, Box 100284 JHMHC, University of Florida, Gainesville, FL 32610, USA

关键词: Arrestin;    S-antigen;    G-protein-linked receptor;    Phosphorylation;    Vision;    Rhodopsin;    cGMP;    guanosine 3′:5′-cyclic monophosphate;    DEAE-cellulose;    diethylaminoethyl cellulose;    DTT;    dithiothreitol;    EDTA;    (ethylenedinitrilo)tetraacetic acid;    HEPES;    (N-[hydroxyethyl]piperazine-N′-[2-ethanesulfonic acid]);    PDE;    cGMP-phosphodiesterase;    PMSF;    phenylmethylsulfonyl fluoride;    ROS;    rod outer segment;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;    7P[330–348];    rhodopsin peptide of sequence 330–348 in which all seven serine and threonine residues are phosphorylated;   

DOI  :  10.1016/0014-5793(95)00225-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A synthetic heptaphosphopeptide comprising the fully phosphorylated carboxyl terminal phosphorylation region of bovine rhodopsin, residues 330–348, was found to induce a conformational change in bovine arrestin. This caused an alteration of the pattern of limited proteolysis of arrestin similar to that induced by binding phosphorylated rhodopsin or heparin. Unlike heparin, the phosphopeptide also induced light-activated binding of arrestin to both unphosphorylated rhodopsin in disk membranes as well as to endoproteinase Asp-N-treated rhodopsin (des 330–348). These findings suggest that one function of phosphorylation of rhodopsin is to activate arrestin which can then bind to other regions of the surface of the photoactivated rhodopsin.

【 授权许可】

Unknown