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• W4321607695 endingPage "22.2023" @default.
• W4321607695 startingPage "ENEURO.0330" @default.
• W4321607695 abstract "Abstract Rhodopsin is the critical receptor molecule which enables vertebrate rod photoreceptor cells to detect a single photon of light and initiate a cascade of molecular events leading to visual perception. Recently, it has been suggested that the F45L mutation in the transmembrane helix of rhodopsin disrupts its dimerization in vitro . To determine whether this mutation of rhodopsin affects its signaling properties in vivo , we generated knock-in mice expressing the rhodopsin F45L mutant. We then examined the function of rods in the mutant mice versus wild-type controls, using in vivo electroretinography and transretinal and single cell suction recordings, combined with morphologic analysis and spectrophotometry. Although we did not evaluate the effect of the F45L mutation on the state of dimerization of the rhodopsin in vivo , our results revealed that F45L-mutant mice exhibit normal retinal morphology, normal rod responses as measured both in vivo and ex vivo , and normal rod dark adaptation. We conclude that the F45L mutation does not affect the signaling properties of rhodopsin in its natural setting." @default.
• W4321607695 created "2023-02-24" @default.
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• W4321607695 date "2023-02-23" @default.
• W4321607695 modified "2023-10-14" @default.
• W4321607695 title "Investigating the Role of Rhodopsin<i>F45L</i>Mutation in Mouse Rod Photoreceptor Signaling and Survival" @default.
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• W4321607695 doi "https://doi.org/10.1523/eneuro.0330-22.2023" @default.
• W4321607695 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36823167" @default.
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