Reining in cytokinesis with a septin corral

Bioessays. 2005 Jan;27(1):5-8. doi: 10.1002/bies.20167.


Septins are a family of conserved GTP-binding proteins that function in cytokinesis in fungi and animals. In budding yeast, septins form scaffolds for assembly of the actomyosin contractile ring at the cleavage plane, a role that does not appear to be conserved in other organisms. The septins form an hourglass-shaped collar at the mother-bud neck, which splits into two rings flanking the division plane at cytokinesis. A recent study(1) demonstrates that these two septin rings constitute diffusion barriers that create a cytokinetic compartment to retain cortical cytokinetic factors in proximity to the cleavage plane.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Cycle Proteins / chemistry
  • Cytokinesis*
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / physiology*
  • Diffusion
  • Fungal Proteins / chemistry
  • GTP Phosphohydrolases / chemistry
  • GTP-Binding Proteins / chemistry
  • Humans
  • Macromolecular Substances / chemistry
  • Models, Biological
  • Saccharomycetales


  • Cell Cycle Proteins
  • Cytoskeletal Proteins
  • Fungal Proteins
  • Macromolecular Substances
  • GTP Phosphohydrolases
  • GTP-Binding Proteins