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PP1 Cooperates with ASPP2 to Dephosphorylate and Activate TAZ.

J Biol Chem.. 2011-02;  286(7):5558 - 5566
Chen-Ying Liu, Xianbo Lv, Tingting Li, Yanping Xu, Xin Zhou, Shimin Zhao, Yue Xiong, Qun-Ying Lei, and Kun-Liang Guan. Key Laboratory of Molecular Medicine, Ministry of Education, Department of Biochemistry and Molecular Biology School of Medicine, Lab, Institutes of Biomedical Sciences, Fudan University, Shanghai 200
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摘要

The Hippo pathway regulates organ size by controlling both cell proliferation and apoptosis. TAZ functions as a transcriptional co-activator downstream of the Hippo pathway and has been implicated in human cancer development. A key step in the Hippo-TAZ pathway is phosphorylation of TAZ by LATS kinase, which leads to TAZ inhibition by both cytoplasmic retention and degradation. However, the mechanism of TAZ dephosphorylation and the responsible phosphatase are unknown. Here, we identified PP1 as a bona fide TAZ phosphatase. PP1A dephosphorylates TAZ at Ser-89 and Ser-311, promotes TAZ nuclear translocation, and stabilizes TAZ by disrupting the binding to the SCF E3 ubiquitin ligase. Furthermore, ASPP2 facilitat... More

关键词

PP1; Protein Stability; Serine/Threonine Protein Phosphatase; Signal Transduction; Transcription Co-activators; ASPP2; Hippo Pathway; TAZ