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Oncogene. 2016 Jan 28;35(4):491-500. doi: 10.1038/onc.2015.106. Epub 2015 Apr 20.

SCP1 regulates c-Myc stability and functions through dephosphorylating c-Myc Ser62.

Wang W1,2, Liao P1,2, Shen M2, Chen T2, Chen Y2, Li Y2, Lin X3, Ge X1, Wang P1,2,4.

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Department of Central Laboratory, Shanghai 10th People's Hospital, Tongji University, Shanghai, China.
Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
Department of Surgery, Baylor College of Medicine, Houston, TX, USA.
School of Life Science and Technology, Tongji University, Shanghai, China.


Serine 62 (Ser62) phosphorylation affects the c-Myc protein stability in cancer cells. However, the mechanism for dephosphorylating c-Myc is not well understood. In this study, we identified carboxyl-terminal domain RNA polymerase II polypeptide A small phosphatase 1 (SCP1) as a novel phosphatase specifically dephosphorylating c-Myc Ser62. Ectopically expressed SCP1 strongly dephosphorylated c-Myc Ser62, destabilized c-Myc protein and suppressed c-Myc transcriptional activity. Knockdown of SCP1 increased the c-Myc protein levels in liver cancer cells. SCP1 interacted with c-Myc both in vivo and in vitro. In addition, Ser245 at the C-terminus of SCP1 was essential for its phosphatase activity towards c-Myc. Functionally, SCP1 negatively regulated the cancer cell proliferation. Collectively, our findings indicate that SCP1 is a potential tumor suppressor for liver cancers through dephosphorylating c-Myc Ser62.

[Indexed for MEDLINE]

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