Some assembly required: yeast septins provide the instruction manual

Trends Cell Biol. 2005 Aug;15(8):414-24. doi: 10.1016/j.tcb.2005.06.007.

Abstract

Septins are a family of conserved proteins that form hetero-oligomeric complexes that assemble into filaments. The filaments can be organized into linear arrays, coils, rings and gauzes. They serve as membrane-associated scaffolds and as barriers to demarcate local compartments, especially for the establishment of the septation site for cytokinesis. Studies in budding and fission yeast have revealed many of the protein-protein interactions that govern the formation of multi-septin complexes. GTP binding and phosphorylation direct the polymerization of filaments that is required for septin-collar assembly in budding yeast, whereas a homolog of anillin instructs timely formation of the ring of septin filaments at the medial cortex in fission yeast. These insights should aid understanding of the organization and function of the diverse septin structures in animal cells.

Publication types

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

MeSH terms

  • Animals
  • Contractile Proteins / metabolism
  • Cytokinesis
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / metabolism*
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / classification
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Schizosaccharomyces / cytology*
  • Schizosaccharomyces / metabolism

Substances

  • Contractile Proteins
  • Multiprotein Complexes
  • Saccharomyces cerevisiae Proteins
  • anillin