Septin Biology and Cellular Dynamics

Septins are a conserved family of GTP-binding cytoskeletal proteins that assemble into filaments, rings and cage-like structures to organise membrane domains, scaffold other cytoskeletal systems and regulate diverse cellular processes. They form hetero-oligomeric complexes whose composition defines higher-order assemblies that guide cytokinesis, control diffusion barriers and coordinate interactions with actin and microtubules. Through nucleotide-dependent conformational changes and binding to curvature-sensitive lipids, septins sculpt membrane topology during cell division, vesicle trafficking and neurite outgrowth. Their dynamic remodelling is modulated by phosphorylation and accessory factors, enabling spatiotemporal control over contractile ring constriction, asymmetric segregation of cellular contents and signal transduction. Dysregulation of septin organisation has been implicated in metabolic disorders, neurodegeneration, infection and cancer, emphasising their global significance as targets for therapeutic intervention and as fundamental players in cellular homeostasis.

Research from Nature Portfolio

Recent studies have revealed how phosphorylation of an F-BAR protein orchestrates septin ring splitting in budding yeast by modulating septin-membrane interactions and promoting actomyosin ring recruitment, thereby driving cytokinesis. In vitro reconstitution experiments have demonstrated that micrometric curvature-sensitive septin filaments actively reshape lipid bilayers, with preferential alignment on convex and concave surfaces, leading to a theoretical model that captures septin-mediated membrane deformations observed in vivo. Foundational work has also shown that the pivotal septin subunit SEPT7 provides a molecular scaffold for HDAC6-mediated deacetylation of microtubules, balancing filament stability to optimise neurite outgrowth and coordinate cross-talk between septin and tubulin networks.

Septin Biology and Cellular Dynamics publication trend

The graph below shows the total number of articles in septin biology and cellular dynamics across all publications each year (not limited to Nature Index journals).

Technical terms

Septins: Family of GTP-binding cytoskeletal proteins that assemble into filaments and rings to regulate cell division, membrane remodelling and compartmentalisation.

GTPase: Enzyme that binds and hydrolyses guanosine triphosphate, controlling septin assembly dynamics through nucleotide-dependent conformational changes.

Hetero-oligomeric complex: Assembly of different septin subunits into tri-, hexa- or octameric structures that underpin higher-order filament formation.

Actomyosin ring: Contractile ring composed of actin filaments and myosin motors that drives membrane constriction during cytokinesis.

Lipolysis: Metabolic process by which triglycerides in adipocytes are broken down into free fatty acids and glycerol.

Diffusion barrier: Membrane or filament-based structure that restricts lateral movement of proteins and lipids to maintain compartmental identity.

References

1. Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast. Nature Communications (2024).
2. Membrane reshaping by micrometric curvature sensitive septin filaments. Nature Communications (2019).
3. Septins promote dendrite and axon development by negatively regulating microtubule stability via HDAC6-mediated deacetylation. Nature Communications (2013).
4. Adipocyte Septin-7 attenuates obesogenic adipogenesis and promotes lipolysis to prevent obesity. Molecular Metabolism (2025).
5. Septins Recognize and Entrap Dividing Bacterial Cells for Delivery to Lysosomes. Cell Host & Microbe (2018).
6. The Mammalian Septin Interactome. Frontiers in Cell and Developmental Biology (2017).