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- W2070564275 abstract "The parathyroid hormone (PTH)/PTH-related peptide (PTHrP) receptor (PTH1R) belongs to family B of seven-transmembrane-spanning receptors and is activated by PTH and PTHrP. Upon PTH stimulation, the rat PTH1R becomes phosphorylated at seven serine residues. Elimination of all PTH1R phosphorylation sites results in prolonged cAMP accumulation and impaired internalization in stably transfected LLC-PK1 cells. The present study explores the role of individual PTH1R phosphorylation sites in PTH1R signaling through phospholipase C, agonist-dependent receptor internalization, and regulation by G protein-coupled receptor kinases. By means of transiently transfected COS-7 cells, we demonstrate that the phosphorylation-deficient (pd) PTH1R confers dramatically enhanced coupling to G q/11 proteins upon PTH stimulation predominantly caused by elimination of Ser 491/492/493 , Ser 501 , or Ser 504 . Reportedly, impaired internalization of the pd PTH1R, however, is not dependent on a specific phosphorylation site. In addition, we show that G protein-coupled receptor kinase 2 interferes with pd PTH1R signaling to G q/11 proteins at least partially by direct binding to G q/11 proteins." @default.
- W2070564275 created "2016-06-24" @default.
- W2070564275 creator A5013053493 @default.
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- W2070564275 date "2008-09-01" @default.
- W2070564275 modified "2023-10-11" @default.
- W2070564275 title "Eliminating phosphorylation sites of the parathyroid hormone receptor type 1 differentially affects stimulation of phospholipase C and receptor internalization" @default.
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- W2070564275 doi "https://doi.org/10.1152/ajpendo.00036.2008" @default.
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