Regulation of the proapoptotic ARTS protein by ubiquitin-mediated degradation

J Biol Chem. 2005 Jul 8;280(27):25802-10. doi: 10.1074/jbc.M501955200. Epub 2005 Apr 18.

Abstract

ARTS is a mitochondrial protein that promotes apoptosis induced by a variety of proapoptotic stimulators. ARTS induces apoptosis, at least in part, through binding to and antagonizing IAPs (inhibitors of apoptosis proteins). As a result of ARTS binding to IAPs, caspase inhibition is removed and apoptosis can be executed. Here we show that high cellular levels of ARTS protein sensitize cells toward apoptosis. Accordingly, in healthy cells ARTS levels are kept low through constant ubiquitin-mediated degradation. Upon proapoptotic stimuli, the ubiquitination process is inhibited, resulting in increased levels of ARTS. Increased ARTS in turn leads to a decrease of Bcl-2 and Bcl-xL protein levels, cytochrome c release from mitochondria and apoptosis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Apoptosis / physiology*
  • COS Cells
  • Chlorocebus aethiops
  • Cytochromes c / metabolism
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism*
  • GTP Phosphohydrolases / genetics
  • GTP Phosphohydrolases / metabolism*
  • HeLa Cells
  • Humans
  • Mitochondria / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Septins
  • Transfection
  • Ubiquitin / metabolism*
  • bcl-X Protein

Substances

  • BCL2L1 protein, human
  • Cytoskeletal Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Ubiquitin
  • bcl-X Protein
  • Cytochromes c
  • GTP Phosphohydrolases
  • SEPTIN4 protein, human
  • Septins