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- W4313366853 abstract "Nonimage-forming vision in mammals is mediated primarily by melanopsin (OPN4)-expressing, intrinsically photosensitive retinal ganglion cells (ipRGCs). In mouse M1-ipRGCs, melanopsin predominantly activates, via Gαq,11,14, phospholipase C-β4 to open transient receptor 6 (TRPC6) and TRPC7 channels. In M2- and M4-ipRGCs, however, a prominent phototransduction mechanism involves the opening of hyperpolarization- and cyclic nucleotide-gated channels via cyclic nucleotide, although the upstream steps remain uncertain. We report here experiments, primarily on M4-ipRGCs, with photo-uncaging of cyclic nucleotides and virally expressed CNGA2 channels to conclude that the second messenger is cyclic adenosine monophosphate (cAMP) - very surprising considering that cyclic guanosine monophosphate (cGMP) is used in almost all cyclic nucleotide-mediated phototransduction mechanisms across the animal kingdom. We further found that the upstream G protein is likewise Gq, which via its Gβγ subunits directly activates adenylyl cyclase (AC). Our findings are a demonstration in a native cell of a cross-motif GPCR signaling pathway from Gq directly to AC with a specific function." @default.
- W4313366853 created "2023-01-06" @default.
- W4313366853 creator A5055328507 @default.
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- W4313366853 creator A5089844848 @default.
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- W4313366853 date "2022-12-29" @default.
- W4313366853 modified "2023-09-30" @default.
- W4313366853 title "Unusual phototransduction via cross-motif signaling from G <sub>q</sub> to adenylyl cyclase in intrinsically photosensitive retinalganglion cells" @default.
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- W4313366853 doi "https://doi.org/10.1073/pnas.2216599120" @default.
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