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- W5113020 abstract "Calcium sensing receptor (CaSR) biosynthesis incorporates quality control checkpoints common to all G protein-coupled receptors as well as a unique conformational checkpoint. The membrane-permeant allosteric agonist NPS R-568 can increase net and surface abundance of wt CaSR and a class of loss-of-function mutants. Here we use [35S]cysteine labeling to characterize the mechanism of NPS R-568 action. [35S]CaSR is cotranslationally glycosylated with slow and incomplete maturation to the final glycosylated form. [35S]CaSR is relatively stable (half-life > 8–12 hrs). Incorporation of [35S]cysteine into CaSR is linear over 60 min and the rate of [35S]CaSR biosynthesis varies as a function of conformation, which can be biased toward the ‘active’ state by cotranslational exposure to NPS R-568 in cells with little or no plasma membrane CaSR. Similar effects on net [35S]CaSR biosynthesis are observed with loss- or gain-of-function mutations. Thus NPS R-568 can cotranslationally regulate [35S]CaSR stability. [35S]cysteine pulse-chase analysis suggests that prolonged exposure to NPS R-568 not only increases cotranslational stability but also facilitates maturation of [35S]CaSR through the secretory pathway. Overall, these results suggest that CaSR is subject to cotranslational quality control which includes a pharmacochaperone-sensitive conformational checkpoint. NIH GM077563 and Geisinger Clinic." @default.
- W5113020 created "2016-06-24" @default.
- W5113020 creator A5006404294 @default.
- W5113020 creator A5058082965 @default.
- W5113020 date "2010-04-01" @default.
- W5113020 modified "2023-10-16" @default.
- W5113020 title "Cotranslational regulation of calcium sensing receptor biosynthesis by an allosteric agonist" @default.
- W5113020 doi "https://doi.org/10.1096/fasebj.24.1_supplement.852.1" @default.
- W5113020 hasPublicationYear "2010" @default.
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