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Related Concept Videos

Septins01:19

Septins

1.6K
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...
1.6K
Role of Septins01:02

Role of Septins

1.5K
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...
1.5K
GTPases and their Regulation02:14

GTPases and their Regulation

7.9K
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,...
7.9K
GTPases and their Regulation02:14

GTPases and their Regulation

2.4K
2.4K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

3.5K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.5K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

8.9K
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...
8.9K

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Related Experiment Video

Updated: May 5, 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

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Human septin isoforms and the GDP-GTP cycle.

Eldar Zent, Alfred Wittinghofer

    Biological Chemistry
    |November 20, 2013
    PubMed
    Summary

    Septin GTPase activity is crucial for filament dynamics. This study reveals how GTP binding and hydrolysis in septin complexes, particularly Sept7, influence their stability and biological functions.

    Area of Science:

    • Molecular Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Septins are GTP-binding proteins forming filaments essential for various cellular processes.
    • The role of the GDP-to-GTP conformational switch in septin filament dynamics remains unclear.
    • Septin oligomerization involves interactions between different septin subgroups.

    Purpose of the Study:

    • To investigate the GTPase reaction of human septin groups.
    • To understand the influence of nucleotide binding on septin dimer and filament stability.
    • To elucidate the specific role of Sept7 in filament formation and dynamics.

    Main Methods:

    • Analysis of the complex GTPase reaction across four human septin groups.
    • Investigation of dimer formation stability via the guanine nucleotide-binding (G) interface.

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    Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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  • Comparison of GTPase activity in monomeric states and the effect of nucleotide exchange on Sept7.

    • Main Results:

    • Dimer formation stability at the G-interface is a key feature of the septin GTPase reaction.
    • Three septin groups exhibit similar GTP hydrolysis in the monomeric state; Sept6 lacks GTPase activity.
    • Sept7 forms a stable GDP-bound G-interface dimer, but triphosphate exchange destabilizes this interface.

    Conclusions:

    • The stability of the Sept7 G-interface dimer is modulated by triphosphate binding, impacting filament dynamics.
    • Septin GTPase activity and conformational switching are critical for regulating septin filament assembly and function.
    • Understanding these mechanisms provides insights into septin-related biological processes and diseases.