Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency

Cell. 2013 Sep 26;155(1):160-71. doi: 10.1016/j.cell.2013.08.032. Epub 2013 Sep 19.

Abstract

Respiratory chain complexes assemble into functional quaternary structures called supercomplexes (RCS) within the folds of the inner mitochondrial membrane, or cristae. Here, we investigate the relationship between respiratory function and mitochondrial ultrastructure and provide evidence that cristae shape determines the assembly and stability of RCS and hence mitochondrial respiratory efficiency. Genetic and apoptotic manipulations of cristae structure affect assembly and activity of RCS in vitro and in vivo, independently of changes to mitochondrial protein synthesis or apoptotic outer mitochondrial membrane permeabilization. We demonstrate that, accordingly, the efficiency of mitochondria-dependent cell growth depends on cristae shape. Thus, RCS assembly emerges as a link between membrane morphology and function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • BH3 Interacting Domain Death Agonist Protein / chemistry
  • BH3 Interacting Domain Death Agonist Protein / metabolism
  • Cell Respiration*
  • Electron Transport*
  • GTP Phosphohydrolases / genetics
  • Humans
  • Mice
  • Mice, Inbred C57BL
  • Mitochondria / chemistry
  • Mitochondria / physiology
  • Mitochondrial Membranes / chemistry
  • Mitochondrial Membranes / physiology*
  • Mitochondrial Membranes / ultrastructure
  • Molecular Sequence Data
  • Multiprotein Complexes / metabolism
  • Sequence Alignment

Substances

  • BH3 Interacting Domain Death Agonist Protein
  • Multiprotein Complexes
  • GTP Phosphohydrolases
  • Opa1 protein, mouse