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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...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Actin Treadmilling01:18

Actin Treadmilling

Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...

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Local PI(4,5)P<sub>2</sub> synthesis by septin-associated PIPKIγ isoforms controls centralspindlin association with the midbody during cytokinesis.

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Related Experiment Video

Updated: Jun 1, 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 pairs, a complex choreography.

Helge Ewers1

  • 1Institute of Biochemistry, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland.

The Journal of Cell Biology
|June 15, 2011
PubMed
Summary
This summary is machine-generated.

Septin proteins form a filamentous collar in yeast during cell division. This study reveals septin complexes assemble as paired filaments, offering new insights into their organization during cytokinesis.

More Related Videos

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

Published on: July 28, 2022

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

Related Experiment Videos

Last Updated: Jun 1, 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

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

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

Published on: July 28, 2022

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
  • Cytoskeletal Dynamics
  • Molecular Cell Biology

Background:

  • Septins are essential cytoskeletal proteins involved in cell division.
  • In budding yeast, septins form a collar at the mother-bud neck, crucial for cytokinesis.
  • The precise organization and assembly of septin complexes during cytokinesis remain incompletely understood.

Purpose of the Study:

  • To investigate the in vivo assembly of septin complexes.
  • To elucidate the organization of septin filaments during the process of cytokinesis.
  • To provide new insights into the dynamic reorientation of septin rings.

Main Methods:

  • Utilized fluorescence polarization microscopy to visualize septin organization in live budding yeast cells.
  • Applied advanced imaging techniques to observe septin complex assembly and dynamics during cytokinesis.

Main Results:

  • Demonstrated that septin complexes assemble as paired filaments in vivo.
  • Observed a dramatic reorientation of septin complexes as the septin collar splits into two rings during cytokinesis.
  • Provided visual evidence for the dynamic assembly and structural rearrangements of septins.

Conclusions:

  • Septin complexes adopt a paired filament structure during their assembly.
  • The findings offer a refined model for septin organization and dynamics throughout the cell division process.
  • This study enhances our understanding of the molecular mechanisms governing cytokinesis in yeast.