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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...
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...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: Jun 6, 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

A draft of the human septin interactome.

Marcel Nakahira1, Joci Neuby Alves Macedo, Thiago Vargas Seraphim

  • 1Laboratório Nacional de Biociências, Centro Nacional de Pesquisa em Energia e Materiais, Campinas, Brasil.

Plos One
|November 18, 2010
PubMed
Summary

This study reveals how septins, proteins crucial for cell structure, assemble into filaments. These findings clarify septin interactions and their roles in various cellular 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

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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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Related Experiment Videos

Last Updated: Jun 6, 2026

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

Published on: June 23, 2022

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

Published on: August 17, 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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Septins are GTPase proteins essential for cytokinesis and cell morphology in eukaryotes, excluding plants.
  • Mammalian septins form homo- and heterooligomeric filaments, with a hetero-trimeric core unit.
  • Septin filaments are hypothesized to act as scaffolds for protein recruitment.

Purpose of the Study:

  • To investigate the interaction network of human septins using yeast two-hybrid screens.
  • To understand the assembly rules and potential functions of septin complexes.

Main Methods:

  • Yeast two-hybrid screens were employed using human septins 1-10.
  • Interaction data was analyzed to identify homo- and heterooligomeric septin assemblies.
  • Functional attribution of non-septin interactors was performed.

Main Results:

  • Predominantly, septins were found to interact with other septins, confirming filament formation.
  • Observed interactions largely followed a "group rule," where septins within the same group can substitute each other in filament structures.
  • Specific preferential interactions were identified between different septin groups (e.g., SEPT6 with SEPT2, SEPT3, and SEPT7).
  • SEPT2 septins uniquely interacted within their own group.
  • Non-septin interactors involved in ubiquitin/sumoylation, microtubular transport, cell division, motility, signaling, endocytosis, and apoptosis were identified.

Conclusions:

  • Septin filament assembly is governed by specific group interactions, maintaining structural integrity.
  • Septin complexes participate in a wide array of cellular functions beyond structural roles.
  • The identified interactions provide insights into the molecular mechanisms underlying septin-mediated cellular processes.