Identifying the SUMO1 modification of FAM122A leading to the degradation of PP2A-Cα by ubiquitin-proteasome system

作者：Fangzhi Fan, Junxing Zhao, Yali Liu, Hongfang Zhao, Lietao Weng, Qingqing Li, Guoqiang Chen, Ying Xu · 发表于：Biochemical and Biophysical Research Communications · 年份：2018 · DOI：10.1016/j.bbrc.2018.04.135 · 被引用次数：5 · 研究领域：Ubiquitin and proteasome pathways、Peptidase Inhibition and Analysis、RNA modifications and cancer

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.