Role of the mitochondrial contact site and cristae organizing system in membrane architecture and dynamics

Biochim Biophys Acta Mol Cell Res. 2017 Apr;1864(4):737-746. doi: 10.1016/j.bbamcr.2016.05.020. Epub 2016 Sep 7.


The elaborate membrane architecture of mitochondria is a prerequisite for efficient respiration and ATP generation. The cristae membranes, invaginations of the inner mitochondrial membrane, represent a specialized compartment that harbors the complexes of the respiratory chain and the F1Fo-ATP synthase. Crista junctions form narrow openings that connect the cristae membranes to the inner boundary membrane. The mitochondrial contact site and cristae organizing system (MICOS) is located at crista junctions where it stabilizes membrane curvature and forms contact sites between the mitochondrial inner and outer membranes. MICOS is a large machinery, consisting of two dynamic subcomplexes that are anchored in the inner membrane and expose domains to the intermembrane space. The functions of MICOS in mitochondrial membrane architecture and biogenesis are influenced by numerous interaction partners and the phospholipid environment.

Keywords: Crista junction; Cristae; MICOS; Mitochondria; Phospholipid.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • DNA, Mitochondrial / genetics*
  • DNA, Mitochondrial / metabolism
  • Gene Expression Regulation
  • Humans
  • Mitochondria / metabolism*
  • Mitochondria / ultrastructure
  • Mitochondrial Membrane Transport Proteins / genetics*
  • Mitochondrial Membrane Transport Proteins / metabolism
  • Mitochondrial Membranes / metabolism*
  • Mitochondrial Membranes / ultrastructure
  • Phospholipids / metabolism
  • Protein Binding
  • Proton-Translocating ATPases / genetics*
  • Proton-Translocating ATPases / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Signal Transduction
  • Species Specificity


  • DNA, Mitochondrial
  • Mitochondrial Membrane Transport Proteins
  • Phospholipids
  • Proton-Translocating ATPases