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

Biochem Biophys Res Commun. 2018 Jun 7;500(3):676-681. doi: 10.1016/j.bbrc.2018.04.135. Epub 2018 Apr 22.

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.

Keywords: FAM122A; PP2A; Phosphatase activity; SUMO1 modification; Ubiquitination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Proliferation
  • HEK293 Cells
  • Humans
  • Lysine / metabolism
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Phosphatase 2 / metabolism*
  • Protein Processing, Post-Translational*
  • Proteolysis*
  • SUMO-1 Protein / metabolism*
  • Sumoylation
  • Ubiquitin / metabolism*

Substances

  • Phosphoproteins
  • SUMO-1 Protein
  • Ubiquitin
  • Protein Phosphatase 2
  • Proteasome Endopeptidase Complex
  • Lysine