Bnip3 as a dual regulator of mitochondrial turnover and cell death in the myocardium

Pediatr Cardiol. 2011 Mar;32(3):267-74. doi: 10.1007/s00246-010-9876-5. Epub 2011 Jan 6.

Abstract

The Bcl-2 adenovirus E1B 19 kDa-interacting protein 3 (Bnip3) is a pro-apoptotic BH3-only protein associated with the pathogenesis of many diseases, including cancer and cardiovascular disease. Studies over the past decade have provided insight into how Bnip3 induces mitochondrial dysfunction and subsequent cell death in cells. More recently, Bnip3 was identified as a potent inducer of autophagy in cells. However, the functional role of Bnip3-mediated autophagy has been difficult to define and remains controversial. New evidence has emerged suggesting that Bnip3 is an important regulator of mitochondrial turnover via autophagy in the myocardium. Also, studies suggest that the induction of Bnip3-dependent mitochondrial autophagy is a separately activated process independent of Bax/Bak and the mitochondrial permeability transition pore (mPTP). This review discusses the current understanding of the functional role that Bnip3 plays in the myocardium. Recent studies suggest that Bnip3 might have a dual function in the myocardium, where it regulates both mitochondrial turnover via autophagy and cell death and that these are two separate processes activated by Bnip3.

Publication types

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

MeSH terms

  • Autophagy / physiology
  • Cell Death / physiology*
  • Humans
  • Membrane Proteins / metabolism*
  • Mitochondria / metabolism*
  • Myocardium / metabolism*
  • Proto-Oncogene Proteins / metabolism*

Substances

  • BNIP3 protein, human
  • Membrane Proteins
  • Proto-Oncogene Proteins