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Related Concept Videos

Septins01:19

Septins

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...
Role of Septins01:02

Role of Septins

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...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...

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Related Experiment Video

Updated: Jun 2, 2026

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

Septin filament formation is essential in budding yeast.

Michael A McMurray1, Aurelie Bertin, Galo Garcia

  • 1Division of Biochemistry and Molecular Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Developmental Cell
|April 19, 2011
PubMed
Summary

Septin filament assembly shows surprising flexibility. Even without key components, septins can form functional filaments, maintaining essential cell division processes.

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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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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins
09:09

Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins

Published on: August 17, 2022

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Septins are GTP-binding proteins crucial for cell division, forming filamentous structures.
  • The precise relationship between septin supramolecular organization and function remained unclear.
  • In Saccharomyces cerevisiae, four septins (Cdc11, Cdc12, Cdc3, Cdc10) form an apolar hetero-octamer that polymerizes into filaments.

Purpose of the Study:

  • To investigate the plasticity of septin filament assembly.
  • To understand how alterations in septin composition affect filament formation and function.
  • To elucidate the role of specific septin subunits in maintaining cell division.

Main Methods:

  • Analysis of Saccharomyces cerevisiae mutants lacking specific septin subunits (cdc10Δ, cdc11Δ).
  • Investigation of septin subunit self-association capabilities (homodimerization via G interface).
  • Microscopic observation of septin localization at the bud neck and assessment of diffusion barrier function.

Main Results:

  • Cells lacking Cdc10 or Cdc11 can still divide, as remaining subunits retain homodimerization ability for filament assembly.
  • These altered septin filaments correctly localize to the bud neck and form diffusion barriers.
  • Mutants unable to self-associate but capable of capping other subunits fail to form filaments, leading to cell death.

Conclusions:

  • Septin filament assembly exhibits significant plasticity, allowing for functional filament formation even with partial subunit composition.
  • The ability of septin subunits to self-associate is critical for filament integrity, cortical localization, and cell viability.
  • This plasticity ensures the maintenance of essential cell division processes through robust diffusion barriers.