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

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.

journal_name

Oncogene

journal_title

Oncogene

authors

Wang W,Liao P,Shen M,Chen T,Chen Y,Li Y,Lin X,Ge X,Wang P

doi

10.1038/onc.2015.106

subject

Has Abstract

pub_date

2016-01-28 00:00:00

pages

491-500

issue

4

eissn

0950-9232

issn

1476-5594

pii

onc2015106

journal_volume

35

pub_type

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