BAX inhibitor-1 regulates autophagy by controlling the IRE1α branch of the unfolded protein response

EMBO J. 2011 Sep 16;30(21):4465-78. doi: 10.1038/emboj.2011.318.

Abstract

Both autophagy and apoptosis are tightly regulated processes playing a central role in tissue homeostasis. Bax inhibitor 1 (BI-1) is a highly conserved protein with a dual role in apoptosis and endoplasmic reticulum (ER) stress signalling through the regulation of the ER stress sensor inositol requiring kinase 1 α (IRE1α). Here, we describe a novel function of BI-1 in the modulation of autophagy. BI-1-deficient cells presented a faster and stronger induction of autophagy, increasing LC3 flux and autophagosome formation. These effects were associated with enhanced cell survival under nutrient deprivation. Repression of autophagy by BI-1 was dependent on cJun-N terminal kinase (JNK) and IRE1α expression, possibly due to a displacement of TNF-receptor associated factor-2 (TRAF2) from IRE1α. Targeting BI-1 expression in flies altered autophagy fluxes and salivary gland degradation. BI-1 deficiency increased flies survival under fasting conditions. Increased expression of autophagy indicators was observed in the liver and kidney of bi-1-deficient mice. In summary, we identify a novel function of BI-1 in multicellular organisms, and suggest a critical role of BI-1 as a stress integrator that modulates autophagy levels and other interconnected homeostatic processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acids / metabolism
  • Animals
  • Autophagy / genetics*
  • Cell Survival / genetics
  • Cells, Cultured
  • Drosophila / genetics
  • Endoribonucleases / metabolism*
  • Endoribonucleases / physiology
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*
  • Mice
  • Organisms, Genetically Modified
  • Phagosomes / genetics
  • Phagosomes / metabolism
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Serine-Threonine Kinases / physiology
  • Saccharomyces cerevisiae / genetics
  • Signal Transduction / genetics
  • Signal Transduction / physiology
  • Starvation / metabolism
  • Transport Vesicles / metabolism
  • Unfolded Protein Response / genetics*
  • Unfolded Protein Response / physiology

Substances

  • Acids
  • Membrane Proteins
  • Tmbim6 protein, mouse
  • Ern1 protein, mouse
  • Protein Serine-Threonine Kinases
  • Endoribonucleases