Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization

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...

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Published inThe Journal of pathology Vol. 226; no. 2; pp. 287 - 299
Main Authors Hall, Peter A, Russell, SE Hilary
Format Journal Article
LanguageEnglish
Published Chichester, UK John Wiley & Sons, Ltd 01.01.2012
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Abstract 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.
AbstractList 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.
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.
Author Russell, SE Hilary
Hall, Peter A
Author_xml – sequence: 1
  givenname: Peter A
  surname: Hall
  fullname: Hall, Peter A
  email: phall@kfshrc.edu.sa
  organization: Departments of Molecular Oncology and Pathology and Laboratory Medicine, King Faisal Specialist Hospital and Research Centre, Riyadh, Saudi Arabia
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  givenname: SE Hilary
  surname: Russell
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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.
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Snippet The septins are a family of GTP‐binding proteins, evolutionarily conserved from yeast through to mammals, with roles in multiple core cellular functions. Here...
The septins are a family of GTP-binding proteins, evolutionarily conserved from yeast through to mammals, with roles in multiple core cellular functions. Here...
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StartPage 287
SubjectTerms Animals
Bacterial Infections - genetics
Brachial Plexus Neuritis - genetics
cytoskeleton
Cytoskeleton - genetics
diffusion barrier
disease
filament
Gene Expression - genetics
Humans
Mammals
membrane
Morphogenesis - genetics
Neoplasms - genetics
Phagocytosis - genetics
polarity
Protein Isoforms - genetics
regulation
septin
Septins - genetics
Septins - metabolism
Septins - physiology
splicing
symmetry
Title Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization
URI https://api.istex.fr/ark:/67375/WNG-CQSM32PH-9/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fpath.3024
https://www.ncbi.nlm.nih.gov/pubmed/21990096
https://search.proquest.com/docview/907997133
Volume 226
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