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Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin
Author(s) -
Puig Jaime,
Arendt Anatol,
Tomson Farol L.,
Abdulaeva Galina,
Miller Ron,
Hargrave Paul A.,
Hugh McDowell J.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00225-x
Subject(s) - rhodopsin , phosphopeptide , arrestin , phosphorylation , proteolysis , biochemistry , chemistry , biophysics , microbiology and biotechnology , biology , retinal , g protein coupled receptor , signal transduction , enzyme
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.