|G protein-coupled receptor kinase 1|
|Locus||Chr. 13 q34|
Rhodopsin kinase (EC 188.8.131.52, cone opsin kinase, G-protein-coupled receptor kinase 1, GPCR kinase 1, GRK1, GRK7, opsin kinase, opsin kinase (phosphorylating), rhodopsin kinase (phosphorylating), RK, STK14) is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction
More on Rhodopsin Kinase
Rhodopsin Kinase is involved in mammalian rod cells specifically with photo transduction and belongs to the family of G coupled-protein receptor kinases. This kinase, referred to as GRK1 is post-translationally modified by farnesylation and α-carboxyl methylation GRK1 phosphorylates rhodopsin, resulting in partial photo-activation of rhodopsin, thus activating the dim flash response. Dim flash response is activated in dim light and its ideal to de-activate the rod cell photoreceptor or rhodopsin over time. GRK1 AND GRK7 exist and are isoforms of rhodopsin kinase. Studies have proven that in mice rod cells, GRK1 has competition with arrestin for the binding site of rhodopsin. Arrestin-1 when bound to rhodopsin inhibits signaling and turns off photo-transduction completely. As is true for many enzymes, rhodopsin kinase is regulated by the activity of other proteins. In this case, it is negatively regulated by recoverin. In the dark state of the rod cells' recoverin inhibits rhodopsin kinase. Specifically, a study has proven that GRK1 acts on the cytoplasmic loops of rhodopsin both the second and third loops. The cytoplasmic loops act specifically where transducin binds to rhodopsin so this allows GRK1 and transducin to compete for the binding site on rhodopsin. With recoverin present, it exists between GRK1 and rhodopsin and it was shown that when bound competition between GRK1 and transducin suppressed.
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