期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 69, 期 9, 页码 1551-1562出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-011-0891-3
关键词
Melanopsin; Phosphorylation; In situ proximity assay
资金
- National Science Foundation [IOS0721608]
- National Eye Institute [R01EY019053]
- NIH [T32 GM066706]
Melanopsin-based phototransduction is involved in non-image forming light responses including circadian entrainment, pupil constriction, suppression of pineal melatonin synthesis, and direct photic regulation of sleep in vertebrates. Given that the functions of melanopsin involve the measurement and summation of total environmental luminance, there would appear to be no need for the rapid deactivation typical of other G-protein coupled receptors. In this study, however, we demonstrate that heterologously expressed mouse melanopsin is phosphorylated in a light-dependent manner, and that this phosphorylation is involved in regulating the rate of G-protein activation and the lifetime of melanopsin's active state. Furthermore, we provide evidence for light-dependent phosphorylation of melanopsin in the mouse retina using an in situ proximity ligation assay. Finally, we demonstrate that melanopsin preferentially interacts with the GRK2/3 family of G-protein coupled receptor kinases through co-immunoprecipitation assays. Based on the complement of G-protein receptor kinases present in the melanopsin-expressing retinal ganglion cells, GRK2 emerges as the best candidate for melanopsin's cognate GRK.
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