The influence of arrestin (48K protein) and rhodopsin kinase on visual transduction.
The shutoff of the phototransduction cascade in retinal rods requires the inactivation of light-activated rhodopsin. The underlying mechanisms were studied in functionally intact detached rod outer segments by testing the effect of either sangivamycin, an inhibitor of rhodopsin kinase, or phytic acid, an inhibitor of 48K protein binding to phosphorylated rhodopsin, on light responses recorded in whole-cell voltage clamp. The results suggest that isomerized rhodopsin is inactivated fully by multiple phosphorylation and that the binding of 48K protein accelerates recovery by quenching partially phosphorylated rhodopsin. Higher concentrations of sangivamycin cause changes in the light response that cannot be explained by selective inhibition of rhodopsin kinase and suggest that other protein kinases are needed for normal rod function.
Palczewski
K
K
R. S. Dow Neurological Sciences Institute, Good Samaritan Hospital, Portland, Oregon 97209.
Rispoli
G
G
Detwiler
P B
PB
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000378:metabolism; D000818:Animals; D000941:Antigens / Q000502:physiology*; D019393:Arrestin; D002417:Cattle; D003956:Dialysis; D004553:Electric Conductivity; D005136:Eye Proteins / Q000502:physiology*; D051606:G-Protein-Coupled Receptor Kinase 1; D008027:Light; D008116:Lizards; D010766:Phosphorylation; D010833:Phytic Acid / Q000494:pharmacology; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000502:physiology*; D011741:Pyrimidine Nucleosides / Q000494:pharmacology; D012243:Rhodopsin / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000502:physiology*; D014785:Vision, Ocular / Q000502:physiology*
D000941:Antigens; D019393:Arrestin; D005136:Eye Proteins; D047428:Protein Kinase Inhibitors; D011741:Pyrimidine Nucleosides; C005699:sangivamycin; D010833:Phytic Acid; D012243:Rhodopsin; D011494:Protein Kinases; D051606:G-Protein-Coupled Receptor Kinase 1; D015106:3',5'-Cyclic-GMP Phosphodiesterases