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Mutations in polycystin-1 (PC1) account for \u223c85% of ADPKD. Here, we showed that wild-type (WT) or mutant PC1 composed of the last five transmembrane (TM) domains and the C-terminus (termed PC1-5TMC) inhibits cell proliferation and protein translation, as well as the downstream effectors of mTOR, consistent with previous reports. Knockdown of B56<jats:italic>\u03b1<\/jats:italic>, a subunit of the protein phosphatase 2A (PP2A) complex, or application of PP2A inhibitor okadaic acid or calyculin A, abolished the inhibitory effect of PC1 and PC1-5TMC on proliferation, indicating that PP2A\/B56<jats:italic>\u03b1<\/jats:italic> mediates the regulation of cell proliferation by PC1. In addition to the phosphorylated S6 and 4EBP1, B56<jats:italic>\u03b1<\/jats:italic> was also downregulated by PC1 and PC1-5TMC. Furthermore, the downregulation of B56<jats:italic>\u03b1<\/jats:italic>, which may be mediated by mTOR but not AKT, can account for the dependence of PC1-inhibited proliferation on PP2A.<\/jats:p>","DOI":"10.1155\/2019\/2582401","type":"journal-article","created":{"date-parts":[[2019,9,19]],"date-time":"2019-09-19T19:30:20Z","timestamp":1568921420000},"page":"1-8","source":"Crossref","is-referenced-by-count":3,"title":["Polycystin-1 Inhibits Cell Proliferation through Phosphatase PP2A\/B56<i>\u03b1<\/i>"],"prefix":"10.1155","volume":"2019","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4036-9788","authenticated-orcid":true,"given":"Yan","family":"Tang","sequence":"first","affiliation":[{"name":"Department of Oncology and Haematology, The Second Hospital, Jilin University, Changchun 130041, China"},{"name":"Membrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, Edmonton T6G 2H7, 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