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Related Concept Videos

Septins01:19

Septins

1.9K
Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Role of Septins01:02

Role of Septins

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
Recent studies have revealed the multifaceted roles of septins in various cellular processes such as cytokinesis, ciliogenesis, and neurogenesis. Septins act as scaffolds and...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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Related Experiment Video

Updated: Sep 12, 2025

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

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Cooperativity in septin polymerization is tunable by ionic strength and membrane adsorption.

Ellysa J D Vogt1, Ian Seim2, Wilton T Snead3

  • 1Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina; Department of Cell Biology, Duke University Medical School, Durham, North Carolina.

Biophysical Journal
|August 9, 2025
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Summary

Septin polymers exhibit salt-dependent cooperative assembly in solution, but membrane binding limits this cooperativity. This versatility in assembly modes influences septin functions and locations within cells.

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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins
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Last Updated: Sep 12, 2025

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins
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Area of Science:

  • Cell biology
  • Biophysics
  • Polymer science

Background:

  • Cells utilize cytoskeletal polymers for essential functions like movement and division.
  • Septins, a fourth cytoskeletal component, play roles in membrane dynamics and cell shape but remain poorly understood.
  • Understanding septin polymerization is crucial due to their link to various human diseases.

Purpose of the Study:

  • To investigate the mechanisms of septin polymer elongation under varying conditions.
  • To determine how membranes influence septin polymerization cooperativity.
  • To explore the assembly behaviors of septins in solution and on lipid bilayers.

Main Methods:

  • Reactive Brownian dynamics simulations to assess membrane-induced cooperativity.
  • Fluorescence correlation spectroscopy to evaluate solution-based filament formation at different salt concentrations.
  • Quantitative microscopy to study septin membrane adsorption and polymerization on planar and curved lipid bilayers.

Main Results:

  • Septins demonstrate salt-dependent cooperative assembly in solution.
  • Membrane binding significantly limits septin polymerization cooperativity.
  • Septin assembly is highly sensitive to extrinsic conditions and substrate properties.

Conclusions:

  • Septin polymerization exhibits characteristics of both isodesmic and cooperative modes.
  • The adaptability of septin assembly to different conditions explains their diverse functions and locations.
  • Extrinsic factors critically regulate septin assembly, impacting cellular processes.