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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...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 

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Related Experiment Video

Updated: Jun 19, 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

GTP-induced conformational changes in septins and implications for function.

Minhajuddin Sirajuddin1, Marian Farkasovsky, Eldar Zent

  • 1Abteilung Strukturelle Biologie, Max-Planck-Institut für molekulare Physiologie, Dortmund, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|October 7, 2009
PubMed
Summary
This summary is machine-generated.

GTP binding and hydrolysis regulate septin filament assembly. This study reveals how nucleotide interactions influence septin protein structure and function, impacting cell division and providing a basis for classifying human 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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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

Related Experiment Videos

Last Updated: Jun 19, 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
  • Structural Biology
  • Biochemistry

Background:

  • Septins are GTP-binding proteins crucial for cell division and function.
  • They form dynamic filaments, but nucleotide's role in their regulation is unclear.
  • Existing low-resolution structures lack detail on G domain assembly and interfaces.

Purpose of the Study:

  • To determine the structural basis of nucleotide regulation in septin function.
  • To investigate how GTP binding affects septin conformation and interfaces.
  • To explore the role of specific residues in GTP hydrolysis and septin assembly.

Main Methods:

  • X-ray crystallography of SEPT2 bound to GppNHp at 2.9 A resolution.
  • Biochemical studies and sequence alignment to identify key residues.
  • Yeast genetics to assess the impact of mutations on septin function.

Main Results:

  • The crystal structure reveals GTP-induced conformational changes at G interfaces, affecting N-terminal helix and NC interface.
  • A conserved threonine residue is implicated in GTP hydrolysis, with mutations causing temperature sensitivity in yeast septins.
  • Conserved G interface residues are essential for specific septin heterodimer formation and cell growth.

Conclusions:

  • GTP binding/hydrolysis and nucleotide identity modulate septin interface stability and filament dynamics.
  • These findings provide structural insights into septin filament assembly and disassembly.
  • The study offers a framework for functionally subdividing human septins.