Effect of rhodopsin C-terminal peptide on photoresponses in functionally intact rod outer segments.
The protein-protein interactions that underlie shut-off of the light-activated rhodopsin were studied using synthetic peptides derived from C-terminal region of the rhodopsin. The photoresponses were recorded in whole-cell voltage clamp from rod outer segments (ROS) that were internally dialyzed with an intracellular solution containing the synthetic peptides. This was the first time that synthetic peptides have been used in functionally intact ROS. None of the tested peptides promoted the shut-off of the photolyzed rhodopsin (R) by stimulating the binding of an activated arrestin to non-phosphorylated R, contrary to what was expected from in vitro experiments (Puig et al. FEBS Lett. 362: 185-188, 1995).
Jindrová
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Department of Physiology and Biophysics, University of Washington, Seattle 98195, USA.
Detwiler
P B
PB
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D019393:Arrestin / Q000378:metabolism; D002147:Calmodulin / Q000494:pharmacology; D002417:Cattle; D007700:Kinetics; D008027:Light; D008116:Lizards; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology*; D010766:Phosphorylation; D010782:Photolysis; D012243:Rhodopsin / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D012374:Rod Cell Outer Segment / Q000502:physiology* / Q000528:radiation effects*; D017385:Sequence Homology
D019393:Arrestin; D002147:Calmodulin; D010446:Peptide Fragments; C013110:metarhodopsins; D000255:Adenosine Triphosphate; D012243:Rhodopsin