The effect of rhodopsin phosphorylation on the light-dependent activation of phosphodiesterase from bovine rod outer segments.
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 suppressed compared with non-phosphorylated ones.
Arshavsky
V Y
VY
Dizhoor
A M
AM
Shestakova
I K
IK
Philippov
P
P
D000818:Animals; D002417:Cattle; D002474:Cell-Free System; D004789:Enzyme Activation / Q000187:drug effects / Q000528:radiation effects; D008027:Light; D010750:Phosphoproteins / Q000494:pharmacology*; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D010766:Phosphorylation; D010786:Photoreceptor Cells / Q000201:enzymology*; D012168:Retinal Pigments / Q000378:metabolism* / Q000494:pharmacology*; D012243:Rhodopsin / Q000378:metabolism* / Q000494:pharmacology*; D012374:Rod Cell Outer Segment / Q000201:enzymology*; D013329:Structure-Activity Relationship
D010750:Phosphoproteins; D012168:Retinal Pigments; D012243:Rhodopsin; D010727:Phosphoric Diester Hydrolases