Growth and division of peroxisomes

Int Rev Cytol. 2006;255:237-90. doi: 10.1016/S0074-7696(06)55005-3.


Peroxisomes are ubiquitous subcellular organelles, which are highly dynamic and display large plasticity in response to cellular and environmental conditions. Novel proteins and pathways that mediate and control peroxisome formation, growth, and division continue to be discovered, and the cellular machineries that act together to regulate peroxisome number and size are under active investigation. Here, advances in the field of peroxisomal dynamics and proliferation in mammals and yeast are reviewed. The authors address the signals, conditions, and proteins that affect, regulate, and control the number and size of this essential organelle, especially the components involved in the division of peroxisomes. Special emphasis is on the function of dynamin-related proteins (DRPs), on Fis1, a putative adaptor for DRPs, on the role of the Pex11 family of peroxisomal membrane proteins, and the cytoskeleton.

Publication types

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

MeSH terms

  • Animals
  • Cytoskeleton / metabolism
  • Dynamins / metabolism
  • Fungal Proteins / metabolism
  • GTP Phosphohydrolases / metabolism
  • Humans
  • Membrane Proteins / metabolism
  • Microtubule-Associated Proteins / metabolism
  • Mitochondria / metabolism
  • Mitochondrial Proteins / metabolism
  • Peroxisome Proliferator-Activated Receptors / agonists
  • Peroxisome Proliferator-Activated Receptors / metabolism*
  • Peroxisome Proliferators / pharmacology
  • Peroxisomes / drug effects
  • Peroxisomes / metabolism*
  • Peroxisomes / physiology
  • Peroxisomes / ultrastructure
  • Yeasts / metabolism*
  • Yeasts / physiology


  • FIS1 protein, human
  • Fungal Proteins
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Mitochondrial Proteins
  • PEX11A protein, human
  • PEX11B protein, human
  • PEX11G protein, human
  • Peroxisome Proliferator-Activated Receptors
  • Peroxisome Proliferators
  • GTP Phosphohydrolases
  • DNM1L protein, human
  • Dynamins