N-α-acetyltransferase 10 protein is a negative regulator of 28S proteasome through interaction with PA28β

FEBS Lett. 2013 Jun 5;587(11):1630-7. doi: 10.1016/j.febslet.2013.04.016. Epub 2013 Apr 26.

Abstract

N-α-acetyltransferase 10 protein (Naa10p) regulates various pathways associated with cancer cell proliferation, metastasis, apoptosis and autophagy. However, its role in protein quality control is unknown. Here, we report that Naa10p is physically associated with proteasome activator 28β (PA28β). Naa10p also interacts with PA28α in a PA28β-dependent manner. Naa10p negatively regulates PA28-dependent chymotrypsin-like proteasome activity in cancer cells and in a cell-free system reconstituted with purified proteins, which is not related to 26S proteasome. Acetyltransferase activity of Naa10p is not required for its effect on chymotrypsin-like proteasome activity. Therefore, our data reveal that Naa10p suppresses 28S proteasome activity through interaction with PA28β.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Sequence
  • Cell Line, Tumor
  • Chymotrypsin / chemistry
  • Humans
  • Kinetics
  • N-Terminal Acetyltransferase A / chemistry
  • N-Terminal Acetyltransferase A / metabolism*
  • N-Terminal Acetyltransferase E / chemistry
  • N-Terminal Acetyltransferase E / metabolism*
  • Peptide Library
  • Proteasome Endopeptidase Complex / chemistry
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Interaction Mapping
  • Protein Processing, Post-Translational
  • Proteolysis

Substances

  • Peptide Library
  • N-Terminal Acetyltransferase A
  • NAA10 protein, human
  • N-Terminal Acetyltransferase E
  • Chymotrypsin
  • PSME2 protein, human
  • Proteasome Endopeptidase Complex