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Article

Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812.

The Journal of biological chemistry - 7 May 2004

Cai Yiqiang, Anyatonwu Georgia, Okuhara Dayne, Lee Kyu-Beck, Yu Zhiheng, Onoe Tamehito, Mei Chang-Lin, Qian Qi, Geng Lin, Wiztgall Ralph, Ehrlich Barbara E, Somlo Stefan

Abstract excerpt

Polycystin-2 (PC-2) is a non-selective cation channel that, when mutated, results in autosomal dominant polycystic kidney disease. In an effort to understand the regulation of this channel, we investigated the role of protein phosphorylation in PC-2 function. We demonstrated the direct incorporation of phosphate into PC-2 in cells and tissues and found that this constitutive phosphorylation occurs at Ser(812), a...

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PMID: 14742446
DOI: 10.1074/jbc.M312031200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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