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• W2952919093 abstract "The calcium-sensing receptor (CaS) is the principal controller of extracellular calcium (Ca²⁺_o) homeostasis and is inhibited in vitro and in vivo by protein kinase C (PKC)-mediated phosphorylation at CaS^T888. However, PKC inhibition enhances signaling even in CaSs lacking Thr-888, suggesting that an additional inhibitory site exists. An apparently equivalent PKC regulatory site in metabotropic glutamate receptor 5 (Ser-839) aligns not with CaS^T888 but instead with CaS^S875, which was not previously considered to be a PKC site. CaS^S875A (nonphosphorylatable) exhibited significantly enhanced Ca²⁺_o sensitivity of both intracellular Ca²⁺ mobilization and extracellular signal-regulated kinase 1/2 activation, whereas the phosphomimetic CaS^S875D mutant exhibited a loss of function. The CaS^S875A/T888A double mutant exhibited even greater Ca²⁺_o sensitivity than CaS^T888A alone, a response no longer enhanced by PKC inhibition. Finally, when expressed in CaS lacking its extracellular domain, the CaS^S875A/T888A double mutation elicited maximal activation even under control conditions, but remained sensitive to negative allosteric modulation [<i>N</i>-(2-hydroxy-3-(2-cyano-3-chlorophenoxy)propyl)-1,1-dimethyl-2-(2-nephthyl)ethylamine] or Ca²⁺_o removal. Therefore, we have now identified CaS^S875 as the missing PKC phosphorylation site that, together with CaS^T888, shapes the CaS signaling that underpins Ca²⁺_o homeostasis. Together with the inactive form of the CaS extracellular domain, these sites attenuate Ca²⁺_o sensitivity to attain appropriate physiologic Ca²⁺_o sensing. <h3>Significance Statement</h3> Serine-875 represents the missing inhibitory PKC phosphorlyation site in CaS that in tandem with Thr-888 controls receptor activity." @default.
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• W2952919093 date "2019-06-12" @default.
• W2952919093 modified "2023-10-18" @default.
• W2952919093 title "Identification of Serine-875 as an Inhibitory Phosphorylation Site in the Calcium-Sensing Receptor" @default.
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• W2952919093 doi "https://doi.org/10.1124/mol.119.116178" @default.
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