The pathobiology of the septin gene family

@article{Hall2004ThePO,
  title={The pathobiology of the septin gene family},
  author={Peter A. Hall and Seongmi Russell},
  journal={The Journal of Pathology},
  year={2004},
  volume={204}
}
  • P. Hall, S. Russell
  • Published 1 November 2004
  • Biology, Medicine
  • The Journal of Pathology
Septins are an evolutionarily conserved group of GTP‐binding and filament‐forming proteins that belong to the large superclass of P‐loop GTPases. While originally discovered in yeast as cell division cycle mutants with cytokinesis defects, they are now known to have diverse cellular roles which include polarity determination, cytoskeletal reorganization, membrane dynamics, vesicle trafficking, and exocytosis. Septin proteins form homo‐ and hetero‐oligomeric polymers which can assemble into… 
Do septins have a role in cancer?
TLDR
This review summarises the essential properties of septins and outlines the accumulating evidence for their involvement in human neoplasia, and may belong to the class of cancer critical genes where alteration in expression profile may underpin their role in neoplAsia as opposed to specific mutational events.
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TLDR
The mammalian septins appear to form a novel network of hetero-polymers that are multi-functional, inter-changeable and respond dynamically to signals that coordinate events at the interface between cytoskeleton and membrane biology.
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TLDR
The structure and functions of septins in general are discussed, the evidence for their presence and roles in the kidney are summarized, and little is known about their role in the kidneys.
[Functional Characterization of Septin Complexes].
TLDR
The structural and functional properties of septins and the regulation of their dynamics are reviewed with special emphasis on the role of septin filaments as a cytoskeletal system and its interaction with actin and microtubule cytOSkeletons.
Functional Characterization of Septin Complexes
Septins belong to a family of conserved GTP-binding proteins found in majority of eukaryotic species except for higher plants. Septins form nonpolar complexes that further polymerize into filaments
The emerging functions of septins in metazoans
TLDR
This work focuses on the emerging roles of vertebrate septins in ciliogenesis, neurogenesis, tumorigenesis and host–pathogen interactions, and discusses whether unifying themes underlie the molecular function of septin in health and disease.
The septin family of GTPases: architecture and dynamics
TLDR
The first detailed structural views of the septin core have emerged and these, along with studies of septin dynamics in vivo, have provided new insight into septin-complex assembly and septin function in vivo.
Protein-protein interaction analysis highlights the role of septins in membrane enclosed lumen and mRNA processing.
TLDR
A protein-protein interaction (PPI) network around human septins is built and some important interactions between molecules involved in the spliceosome with septin 2 and septin 7 in particular are highlighted.
Expression profiling the human septin gene family
TLDR
Perturbation of septin expression was widespread in disease and tumours of the various tissues examined, particularly for conditions of the CNS, where alterations in all 13 septin genes were identified.
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References

SHOWING 1-10 OF 211 REFERENCES
Novel roles for mammalian septins: from vesicle trafficking to oncogenesis.
TLDR
A classification for the mammalian septins is suggested based on the sequence homologies in their highly divergent N- and C-termini, which suggest these proteins might be crucial elements for the spatial and/or temporal control of diverse cellular functions.
Properties of SEPT9 isoforms and the requirement for GTP binding
TLDR
The expression patterns of Sept9 protein are very varied in a panel of tumour cell lines and the functional studies are consistent with a model of septin function as a component of a molecular scaffold that contributes to diverse cellular functions.
Assembly of mammalian septins.
TLDR
An immediate goal of septin biochemistry is to define the mechanisms of assembly and disassembly of this elusive cytoskeleton.
Septins: A Highly Conserved Family of Membrane-Associated GTPases with Functions in Cell Division and Beyond
  • W. Trimble
  • Medicine, Biology
    The Journal of Membrane Biology
  • 1999
TLDR
More recent genetic and biochemical studies which hint at septins functions are focused on, and some speculation about their possible roles in cytokinesis and other cellular processes particularly in animal cells is provided.
Roles of septins in the mammalian cytokinesis machinery.
TLDR
Growing evidence suggests that mammalian septins functionally or physically interact with diverse molecules such as actin, actin-binding proteins, proteins of membrane fusion machinery, Cdc42 adapter proteins, a ubiquitin-protein ligase, and phosphoinositides, and careful integration of these data may provide insights into the mechanism of mammalian septin organization and functions in cytokinesis.
Molecular Dissection of a Yeast Septin: Distinct Domains Are Required for Septin Interaction, Localization, and Function
TLDR
It is found that septins are multifunctional proteins with specific domains involved in distinct molecular interactions required for assembly, localization, and function within the cell.
Borg/Septin Interactions and the Assembly of Mammalian Septin Heterodimers, Trimers, and Filaments*
TLDR
It is shown that stable, soluble septin heterodimers can be produced by co-expression from bicistronic vectors in bacteria and that the co- expression of three septins results in their assembly into filaments.
Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
TLDR
The results indicate that the interaction of septins with PtdInsP(2) might be an important cellular mechanism for the spatial and temporal control of septin accumulation.
Biochemical and cell biological characterization of a mammalian septin, Sept11
TLDR
Immunofluorescent study revealed cell type‐dependent intracellular localization of the protein; Sept11 was colocalized dominantly with microtubules and actin stress fibers in HMEC cells and REF52 cells, respectively, and their filamentous distribution was dependent on the cytoskeleton structures with which the protein is colocalization.
GTP Binding Induces Filament Assembly of a Recombinant Septin
TLDR
Re reconstituted filament assembly in vitro by using a recombinant Xenopus septin, Xl Sept2, and results imply that the growth or stability of septin filaments, or both, is regulated by the state of bound nucleotide.
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