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- W2022209112 abstract "PKD2 is mutated in 15% of patients with autosomal dominant polycystic kidney disease. The PKD2 protein, polycystin-2 or TRPP2, is a nonselective Ca 2+ -permeable cation channel that has been shown to function at several locations, including primary cilia, basolateral membrane, and at the endoplasmic reticulum (ER). Nevertheless, the factors that regulate the channel activity of polycystin-2 are not well understood. Polycystin-2 has been shown previously to be regulated by phosphorylation at two serine residues (Ser 812 and Ser 76 ) with distinct functional consequences. Here, we report the identification of a previously unrecognized phosphorylation site within the polycystin-2 C terminus (Ser 801 ), and we demonstrate that it is phosphorylated by protein kinase D. Phosphorylation at this site was significantly increased in response to serum and epidermal growth factor stimulation. In nonciliated Madin-Darby canine kidney I cells, inducible expression of polycystin-2 inhibited cell proliferation compared with wild-type cells. Mutagenesis at Ser 801 abolished these effects and reduced ATP-stimulated Ca 2+ release from ER stores. Finally, we show that a pathogenic mutation (S804N) within the consensus kinase recognition sequence abolished Ser 801 phosphorylation. These results suggest that growth factor-stimulated, protein kinase D-mediated phosphorylation of polycystin-2 is essential for its ER channel function and links extracellular stimuli to its effects on cell growth and intracellular calcium regulation." @default.
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- W2022209112 date "2010-11-15" @default.
- W2022209112 modified "2023-09-27" @default.
- W2022209112 title "Protein Kinase D–mediated Phosphorylation of Polycystin-2 (TRPP2) Is Essential for Its Effects on Cell Growth and Calcium Channel Activity" @default.
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- W2022209112 doi "https://doi.org/10.1091/mbc.e10-04-0377" @default.
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