Literature DB >> 29678583

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

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.
Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.

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


  1 in total

1.  FAM122A promotes acute myeloid leukemia cell growth through inhibiting PP2A activity and sustaining MYC expression.

Authors:  Man-Hua Liu; Jing Chen; Yun-Sheng Yang; Yin-Qi Wang; Guo-Qiang Chen; Yu Zhang; Ying Huang
Journal:  Haematologica       Date:  2021-03-01       Impact factor: 9.941

  1 in total

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