| Literature DB >> 25893300 |
W Wang1,2, P Liao1,2, M Shen2, T Chen2, Y Chen2, Y Li2, X Lin3, X Ge1, P Wang1,2,4.
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.Entities:
Mesh：
Substances：
Year: 2015 PMID： 25893300 DOI： 10.1038/onc.2015.106
Source DB: PubMed Journal: Oncogene ISSN： 0950-9232 Impact factor: 9.867