| Literature DB >> 29678583 |
Fangzhi Fan1, Junxing Zhao2, Yali Liu3, Hongfang Zhao3, Lietao Weng1, Qingqing Li2, Guoqiang Chen4, Ying Xu5.
Abstract
FAM122A is a highly conserved protein in mammals. Here, we identify that FAM122A can be sumoylated at lysine 89, which can be de-conjugated by SENP1. Furthermore, the sumoylation of FAM122A reduces the PP2A-Cα protein level together with the reduced phosphatase activity of PP2A, which suppresses cell proliferation. Collectively, our results suggest that the sumoylation of FAM122A may have a significant role in cellular function.Entities:
Keywords: FAM122A; PP2A; Phosphatase activity; SUMO1 modification; Ubiquitination
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Year: 2018 PMID: 29678583 DOI: 10.1016/j.bbrc.2018.04.135
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575