PT  - JOURNAL ARTICLE
AU  - Deepak Poria
AU  - Alexander V. Kolesnikov
AU  - Tae Jun Lee
AU  - David Salom
AU  - Krzysztof Palczewski
AU  - Vladimir J. Kefalov
TI  - Investigating the Role of Rhodopsin <em>F45L</em> Mutation in Mouse Rod Photoreceptor Signaling and Survival
AID  - 10.1523/ENEURO.0330-22.2023
DP  - 2023 Mar 01
TA  - eneuro
PG  - ENEURO.0330-22.2023
VI  - 10
IP  - 3
4099  - http://www.eneuro.org/content/10/3/ENEURO.0330-22.2023.short
4100  - http://www.eneuro.org/content/10/3/ENEURO.0330-22.2023.full
SO  - eNeuro2023 Mar 01; 10
AB  - 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.