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• W2000481861 abstract "Light-dependent translocation of invertebrate visual guanine-nucleotide binding protein, iG q α, from rhabdomeric membranes to the cytoplasm is one of many mechanisms that contribute to light adaptation in the invertebrate eye. We have previously cloned iG q α from a Loligo pealei photoreceptor cDNA library and shown that when expressed in HEK 293T cells it is palmitoylated. In this study we compared the activation, cytoplasmic translocation, and turnover of iG q α with that of a non-palmitoylated mutant, iG q α(C3,4A). In the HEK 293T cells, muscarinic M1 receptors coupled equally well to iG q α and iG q α(C3,4A) to activate phospholipase C. Activation of iG q α(C3,4A), but not iG q α, induced translocation of the α subunit from the membrane to cytosol with rapid degradation of the soluble protein resulting in a decreased half-life for iG q α(C3,4A) of 10 hours compared to 20 hours for iG q α. Degradation of iG q α(C3,4A) was inhibited by proteasomal inhibitors but not by inhibitors of lysosomal proteases or calpain. The presence of the proteasomal inhibitor led to the accumulation of polyubiquitinated species of either iG q α or iG q α(C3,4A). Our results suggest that palmitoylation of iG q α is required to maintain membrane association of the protein in its active conformation, and whereas membrane-bound and soluble iG q α can be polyubiquitinated, membrane association protects the protein from rapid degradation by the proteasomal pathway." @default.
• W2000481861 created "2016-06-24" @default.
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• W2000481861 date "2007-03-01" @default.
• W2000481861 modified "2023-10-18" @default.
• W2000481861 title "Degradation of the non-palmitoylated invertebrate visual guanine-nucleotide binding protein, iGqα(C3,4A), by the ubiquitin-proteasomal pathway is regulated by its activation and translocation to the cytoplasm" @default.
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• W2000481861 doi "https://doi.org/10.1017/s0952523807070216" @default.
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