Conflict of interest. Peter Hall is Editor-in-Chief of the Journal of Pathology but recused himself (as is Journal policy) from all parts of the handling, peer review and acceptance procedures of this review, which was commissioned by the Guest Editors of the 2012 Annual Review issue.
Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization†
Article first published online: 23 NOV 2011
Copyright © 2011 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.
The Journal of Pathology
Special Issue: The Cell Biology of Disease
Volume 226, Issue 2, pages 287–299, January 2012
How to Cite
Hall, P. A. and Russell, S. H. (2012), Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization. J. Pathol., 226: 287–299. doi: 10.1002/path.3024
- Issue published online: 1 DEC 2011
- Article first published online: 23 NOV 2011
- Accepted manuscript online: 12 OCT 2011 05:26AM EST
- Manuscript Revised: 3 OCT 2011
- Manuscript Accepted: 3 OCT 2011
- Manuscript Received: 19 SEP 2011
- diffusion barrier;
The septins are a family of GTP-binding proteins, evolutionarily conserved from yeast through to mammals, with roles in multiple core cellular functions. Here we provide an overview of our current knowledge of septin structure and function and focus mainly on mammalian septins, but gain much insight by drawing on knowledge of septins in other organisms. We describe their genomic and transcriptional complexity: a complexity manifest also in the diversity of scaffold structures that septins can form. Septin complexes can act to localize interacting proteins at specific intracellular locales and can also define membrane compartments by defining diffusion barriers. By such activities, septins can contribute to the definition of spatial asymmetry and cell polarity and we suggest a potential role in stem cell biology. Finally, we review the evidence that septins contribute to various disease states and argue that it is a breakdown in the tight regulation of their expression (particularly of individual isoforms), and also their inherent ability to oligomerize, which is pathogenic. Study of the perturbation of septin complex formation in disease will provide valuable insights into septin biology and will be a fertile ground for study. Copyright © 2011 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.