Mitochondrial morphology-emerging role in bioenergetics

Free Radic Biol Med. 2012 Dec 15;53(12):2218-28. doi: 10.1016/j.freeradbiomed.2012.09.035. Epub 2012 Sep 29.

Abstract

Dynamic change in mitochondrial shape is a cellular process mediated mainly by fission and fusion of mitochondria. Studies have shown that mitochondrial fission and fusion are directly and indirectly associated with mitochondrial maintenance, bioenergetic demand, and cell death. Changes in mitochondrial morphology are frequently observed in response to changes in the surrounding cellular milieu, such as metabolic flux, that influence cellular bioenergetics. Connections between morphological regulation and the bioenergetic status of mitochondria are emerging as reciprocally responsive processes, though the nature of the signaling remains to be defined. Given the pivotal role mitochondria play in cellular fate, tight regulation of fission and fusion is therefore critical to preserving normal cellular physiology. Here we describe recent advancements in the understanding of the mechanisms governing mitochondrial morphology and their emerging role in mitochondrial bioenergetics.

Keywords: Bioenergetics; DLP1; Drp1; Fission; Free radicals; Fusion; GTPase; Mfn; Mitochondria; Mitochondrial dynamics; Mitochondrial morphology; OPA1; Reactive oxygen species.

Publication types

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

MeSH terms

  • Animals
  • Dynamins
  • Energy Metabolism*
  • GTP Phosphohydrolases / genetics
  • GTP Phosphohydrolases / metabolism
  • Humans
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism
  • Mitochondria / physiology*
  • Mitochondria / ultrastructure
  • Mitochondrial Dynamics
  • Mitochondrial Membranes / metabolism
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism
  • Organelle Shape
  • Reactive Oxygen Species
  • Signal Transduction

Substances

  • Microtubule-Associated Proteins
  • Mitochondrial Proteins
  • Reactive Oxygen Species
  • GTP Phosphohydrolases
  • DNM1L protein, human
  • Dynamins