Septins: the fourth component of the cytoskeleton

@article{Mostowy2012SeptinsTF,
  title={Septins: the fourth component of the cytoskeleton},
  author={Serge Mostowy and Pascale Cossart},
  journal={Nature Reviews Molecular Cell Biology},
  year={2012},
  volume={13},
  pages={183-194}
}
Septins belong to a family of proteins that is highly conserved in eukaryotes and is increasingly recognized as a novel component of the cytoskeleton. All septins are GTP-binding proteins that form hetero-oligomeric complexes and higher-order structures, including filaments and rings. Recent studies have provided structural information about the different levels of septin organization; however, the crucial structural determinants and factors responsible for septin assembly remain unclear… Expand
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 filamentsExpand
[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. Expand
Septins: Cytoskeletal Filaments with Structural and Regulatory Functions
Dubbed as the fourth component of the cytoskeleton, septins comprise a network of nonpolar hetero-polymeric filaments, which assemble in a guanosine nucleotide-dependent manner. Septins areExpand
The state of the septin cytoskeleton from assembly to function.
TLDR
Some of the recent developments in the field of septins remain relatively poorly understood compared with other cytoskeletal proteins but are highlighted. Expand
Septin filament organization in Saccharomyces cerevisiae
TLDR
This work is working towards dissecting the properties of septins from the budding yeast Saccharomyces cerevisiae, where they were first discovered as cell cycle mutants. Expand
Septins in kidney: A territory little explored
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. Expand
Septin Self-Assembly: Plasticity and Protein Scaffolding
TLDR
The mechanism by which septins serve as a protein scaffold for the cell-cycle regulator Hsl1, an AMPK protein kinase that appears to act as sensor for septin assembly is examined, providing evidence that phosphorylation regulates septin self-assembly. Expand
Architecture, remodeling, and functions of the septin cytoskeleton
TLDR
This mini‐review highlights many of the recent findings in septin architecture, remodeling, and function in many cell types with an emphasis on the budding yeast model. Expand
Revisiting SEPT7 and the slippage of β-strands in the septin family.
TLDR
Two high-resolution structures of the SEPT7 GTPase domain complexed with GDP are presented and one of these reveals a previously unreported coordination for the magnesium ion involving four water molecules and only a tenuous connection to the protein. Expand
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. Expand
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References

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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. Expand
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. Expand
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. Expand
Some assembly required: yeast septins provide the instruction manual.
TLDR
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. Expand
Diversity of septin scaffolds.
  • M. Kinoshita
  • Biology, Medicine
  • Current opinion in cell biology
  • 2006
TLDR
The septin system might be redefined as discrete scaffolds that are conditionally united to behave like cytoskeleton, being diverse, discontinuous and relatively static. Expand
The pathobiology of the septin gene family
TLDR
It is posited that septins can act as regulatable scaffolds where the stoichiometry of septin associations, modifications, GTP status, and the interactions with other proteins allow the regulation of key cellular processes including polarity determination. Expand
Characterization of human septin interactions
Abstract Septins constitute a group of GTP binding proteins that assemble into homo- and hetero-oligomeric complexes and filaments. These higher order septin structures are thought to function likeExpand
Structural insight into filament formation by mammalian septins.
TLDR
The structures reveal a universal bipolar polymer building block, composed of an extended G domain, which forms oligomers and filaments by conserved interactions between adjacent nucleotide-binding sites and/or the amino- and carboxy-terminal extensions. Expand
Structural and biochemical properties of Sept7, a unique septin required for filament formation
TLDR
The structure and biochemistry ofSept7 provide new insights into the dynamics of the G interface and outline the differences in the properties of Sept7 compared to the members of group 2 septins. Expand
GTP-induced conformational changes in septins and implications for function
TLDR
It is proposed that GTP binding/hydrolysis and the nature of the nucleotide influence the stability of interfaces in heterooligomeric and polymeric septins and are required for proper septin filament assembly/disassembly. Expand
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