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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.

Author information

1
Department of Central Laboratory, Shanghai 10th People's Hospital, Tongji University, Shanghai, China.
2
Shanghai Key Laboratory of Regulatory Biology, Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai, China.
3
Department of Surgery, Baylor College of Medicine, Houston, TX, USA.
4
School of Life Science and Technology, Tongji University, Shanghai, China.

Abstract

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.

PMID:
25893300
DOI:
10.1038/onc.2015.106
[Indexed for MEDLINE]

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