Septin structure and function in yeast and beyond

Trends Cell Biol. 2011 Mar;21(3):141-8. doi: 10.1016/j.tcb.2010.11.006. Epub 2010 Dec 20.


Septins are conserved GTP-binding proteins that assemble into hetero-oligomeric complexes and higher-order structures such as filaments, rings, hourglasses or gauzes. Septins are usually associated with a discrete region of the plasma membrane and function as a cell scaffold or diffusion barrier to effect cytokinesis, cell polarity, and many other functions. Recent structural studies of septin complexes have provided mechanistic insights into septin filament assembly, but key questions concerning the assembly, dynamics, and function of different septin structures remain to be answered.

Publication types

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

MeSH terms

  • Animals
  • Cell Cycle
  • Cell Polarity
  • Diffusion
  • Humans
  • Protein Binding
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Septins / chemistry*
  • Septins / metabolism*
  • Septins / ultrastructure


  • Septins