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).

• MeSH
• Adenosine Triphosphate pharmacology   MeSH
• Arrestin metabolism   MeSH
• Phosphorylation MeSH
• Photolysis MeSH
• Lizards MeSH
• Calmodulin pharmacology   MeSH
• Kinetics MeSH
• Molecular Sequence Data MeSH
• Peptide Fragments chemistry   pharmacology   MeSH
• Rhodopsin analogs & derivatives   chemistry   metabolism   pharmacology   MeSH
• Amino Acid Sequence MeSH
• Sequence Homology MeSH
• Cattle MeSH
• Light * MeSH
• Rod Cell Outer Segment physiology   radiation effects   MeSH
• Animals MeSH
• Check Tag
• Cattle MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, U.S. Gov't, P.H.S. MeSH
• Names of Substances
• Adenosine Triphosphate MeSH
• Arrestin MeSH
• Calmodulin MeSH
• metarhodopsins MeSH Browser
• Peptide Fragments MeSH
• Rhodopsin MeSH