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• W1987183910 abstract "The dynamics of G protein-mediated signal transduction depend on the two-dimensional diffusion of membrane-bound G proteins and receptors, which has been suggested to be rate-limiting for vertebrate phototransduction, a highly amplified G protein-coupled signaling pathway. Using fluorescence recovery after photobleaching (FRAP), we measured the diffusion of the G protein transducin alpha-subunit (Galpha(t)) and the G protein-coupled receptor rhodopsin on disk membranes of living rod photoreceptors from transgenic Xenopus laevis. Treatment with either methyl-beta-cyclodextrin or filipin III to disrupt cholesterol-containing lipid microdomains dramatically accelerated diffusion of Galpha(t) in its GTP-bound state and of the rhodopsin-Galphabetagamma(t) complex but not of rhodopsin or inactive GDP-bound Galphabetagamma. These results imply an activity-dependent sequestration of G proteins into cholesterol-dependent lipid microdomains, which limits diffusion and exclude the majority of free rhodopsin and the free G protein heterotrimer. Our data offer a novel demonstration of lipid microdomains in the internal membranes of living sensory neurons." @default.
• W1987183910 created "2016-06-24" @default.
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• W1987183910 date "2008-10-01" @default.
• W1987183910 modified "2023-10-13" @default.
• W1987183910 title "Activation-dependent Hindrance of Photoreceptor G Protein Diffusion by Lipid Microdomains" @default.
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• W1987183910 doi "https://doi.org/10.1074/jbc.m803953200" @default.
• W1987183910 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2573089" @default.
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