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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 Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...

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Related Experiment Video

Updated: May 31, 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

Characterization of human septin interactions.

Kirstin Sandrock1, Ingrid Bartsch, Susanne Bläser

  • 1Department of Pediatrics and Adolescent Medicine, University Medical Center Freiburg, Freiburg, Germany.

Biological Chemistry
|July 20, 2011
PubMed
Summary

Researchers identified large-scale human hetero-trimeric septin complexes, revealing SEPT9

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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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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

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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

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 GTP-binding proteins forming filaments and complexes.
  • These structures act as scaffolds and diffusion barriers, regulating cell polarity and cell cycle.
  • Understanding septin interactions is crucial for cellular function.

Purpose of the Study:

  • To extensively characterize septin interaction partners.
  • To identify large-scale human hetero-trimeric septin complexes.
  • To elucidate the role of SEPT9 in septin complex formation and regulation.

Main Methods:

  • Yeast two-hybrid and three-hybrid systems.
  • Precipitation analyses in platelets.
  • Mutagenic analyses of SEPT7.

Main Results:

  • Identification of large-scale human hetero-trimeric septin complexes.
  • Demonstration of SEPT9's role in forming hetero-trimeric complexes.
  • SEPT9 can substitute for SEPT2 group septins and partially for SEPT7.
  • Mutation of SEPT7 phosphorylation site (Y318) affects septin interactions.
  • Identification of septin-septin interactions in platelets.

Conclusions:

  • Hetero-trimeric septin complexes are a significant feature of septin organization.
  • SEPT9 plays a key role in the assembly of these complexes.
  • Septin phosphorylation, specifically at SEPT7 Y318, is a regulatory mechanism.
  • Diverse septin complexes likely regulate platelet function.