Rhodopsin phosphorylation and its role in photoreceptor function.
Light-stimulated phosphorylation of rhodopsin was first described 25 years ago. This paper reviews the progress that has been made towards (i) understanding the nature of the enzymes that phosphorylate and dephosphorylate rhodopsin (ii) identifying the sites of phosphorylation on rhodopsin and (iii) understanding the physiological importance of rhodopsin phosphorylation. Many important questions related to rhodopsin phosphorylation remain unanswered and new strategies and methods are needed to address issues such as the roles of Ca2+ and recoverin. We present one such method that uses mass spectrometry to quantitate rhodopsin phosphorylation in intact mouse retinas.
Department of Biochemistry, University of Washington, Seattle 98195, USA. jbhhh@u.washington.edu
J B
JB
Hurley
M
M
Spencer
G A
GA
Niemi
D000818:Animals; D019393:Arrestin / Q000378:metabolism; D002118:Calcium / Q000502:physiology; D004789:Enzyme Activation; D005136:Eye Proteins; D051606:G-Protein-Coupled Receptor Kinase 1; D008401:Gas Chromatography-Mass Spectrometry; D008027:Light; D051379:Mice; D008815:Mice, Inbred Strains; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D017949:Retinal Cone Photoreceptor Cells / Q000378:metabolism / Q000502:physiology*; D012243:Rhodopsin / Q000378:metabolism*
D019393:Arrestin; D005136:Eye Proteins; D012243:Rhodopsin; D011494:Protein Kinases; D051606:G-Protein-Coupled Receptor Kinase 1; C496762:Grk1 protein, mouse; D002118:Calcium