Research Papers:

FAM122A, a new endogenous inhibitor of protein phosphatase 2A

Li Fan, Man-Hua Liu, Meng Guo, Chuan-Xi Hu, Zhao-Wen Yan, Jing Chen, Guo-Qiang Chen and Ying Huang _

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Oncotarget. 2016; 7:63887-63900. https://doi.org/10.18632/oncotarget.11698

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Li Fan1, Man-Hua Liu1, Meng Guo2, Chuan-Xi Hu2, Zhao-Wen Yan2, Jing Chen1, Guo-Qiang Chen1,2, Ying Huang2

1Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Rui-Jin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China

2Institute of Health Sciences, Shanghai Institutes for Biological Sciences of Chinese Academy of Sciences and Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China

Correspondence to:

Ying Huang, email: [email protected]

Guo-Qiang Chen, email: [email protected]

Keywords: FAM122A, PP2A, ubiquitination, phosphatase activity, cell growth

Received: March 29, 2016     Accepted: August 24, 2016     Published: August 30, 2016


The regulation of the ubiquitously expressed protein phosphatase 2A (PP2A) is essential for various cellular functions such as cell proliferation, transformation, and fate determination. In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interacts with PP2A-Aα and B55α rather than B56α subunits, and inhibits the phosphatase activity of PP2A-Aα/B55α/Cα complex. Further, FAM122A potentiates the degradation of catalytic subunit PP2A-Cα with the increased poly-ubiquitination. In agreement, FAM122A silencing inhibits while its overexpression enhances cell growth and colony-forming ability. Collectively, we identify FAM122A as a new endogenous PP2A inhibitor and its physiological and pathophysiological significances warrant to be further investigated.

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