title: Rhodopsin phosphorylation: from terminating single photon responses to photoreceptor dark adaptation.
abstract: Rhodopsin phosphorylation has provided one of the first examples of the ubiquitous regulatory pattern of specific kinases downregulating the activity of G-protein-coupled receptors. However, only recently have studies in living animals allowed us to consider the role of rhodopsin phosphorylation in a broader spectrum of visual functions, ranging from the ability of rods to generate reproducible electrical responses to their ability to adapt to darkness after substantial light exposures.
authors.affiliation: Dept of Ophthalmology, Harvard Medical School and the Massachusetts Eye and Ear Infirmary, Boston, MA 02114, USA. vadim_arshavsky@meei.harvard.edu
authors.forename: Vadim Y
authors.initials: VY
authors.lastname: Arshavsky
mesh_terms: D000818:Animals; D019393:Arrestin / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D003623:Dark Adaptation / Q000502:physiology*; D005136:Eye Proteins; D051606:G-Protein-Coupled Receptor Kinase 1; D006801:Humans; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D017948:Retinal Rod Photoreceptor Cells / Q000378:metabolism* / Q000648:ultrastructure; D012243:Rhodopsin / Q000378:metabolism*; D014785:Vision, Ocular / Q000502:physiology*
chemical_list: D019393:Arrestin; D005136:Eye Proteins; D012243:Rhodopsin; D011494:Protein Kinases; D051606:G-Protein-Coupled Receptor Kinase 1; C496764:GRK1 protein, human