The effect of rhodopsin phosphorylation on the light-dependent activation of phosphodiesterase from bovine rod outer segments

• Published in: FEBS letters Vol. 181; no. 2; pp. 264 - 266
• Main Authors: Arshavsky, V.Yu, Dizhoor, A.M., Shestakova, I.K., Philippov, P.P.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 25-02-1985; Elsevier
• Subjects: Animals; Biological and medical sciences; Cattle; Cell physiology; Cell-Free System; Enzyme Activation - drug effects; Enzyme Activation - radiation effects; Fundamental and applied biological sciences. Psychology; Light; Light-dependent phosphodiesterase; Molecular and cellular biology; PDE, cyclic nucleotide phosphodiesterase; phosphodiesterase; Phosphoproteins - pharmacology; Phosphoric Diester Hydrolases - metabolism; Phosphorylation; Photoreceptor Cells - enzymology; Retinal Pigments - metabolism; Retinal Pigments - pharmacology; rhodopsin; Rhodopsin - metabolism; Rhodopsin - pharmacology; Rhodopsin phosphorylation; Rod Cell Outer Segment - enzymology; rod outer segment membranes; ROS, rod outer segments; Structure-Activity Relationship; TD, transducin; Vision, photoreception; Light-dependent phosphodiesterase; ROS, rod outer segments; PDE, cyclic nucleotide phosphodiesterase; TD, transducin; Rhodopsin phosphorylation; Disk membrane; Phosphorylation; Rhodopsin; Enzyme; Photoactivation; Retina; Activation
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(85)80272-6

ATP quenches light-dependent phosphodiesterase (PDE) activation in rod outer segments presumably due to rhodopsin phosphorylation. Here we compared the efficiency of phosphorylated and non-phosphorylated rhodopsins as PDE activators in a reconstituted cell-free system. It is shown that the ability of phosphorylated membranes to activate this enzyme is supressed compared with non-phosphorylated ones.