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
Oncogenejournal_title
Oncogeneauthors
Wang W,Liao P,Shen M,Chen T,Chen Y,Li Y,Lin X,Ge X,Wang Pdoi
10.1038/onc.2015.106subject
Has Abstractpub_date
2016-01-28 00:00:00pages
491-500issue
4eissn
0950-9232issn
1476-5594pii
onc2015106journal_volume
35pub_type
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