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Published on: November 11, 2018
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Septins: Active GTPases or just GTP-binding proteins?
Megha Abbey1, Matthias Gaestel1, Manoj B Menon1
1Hannover Medical School, Institute of Cell Biochemistry, Hannover, 30625, Germany.
Cytoskeleton (Hoboken, N.J.)
|May 11, 2018
Summary
Septins, cytoskeletal proteins, assemble into filaments and rings. This review critically assesses the role of GTP-binding and hydrolysis in septin assembly and function, exploring therapeutic targets.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Septins are essential cytoskeletal proteins involved in cell division and shape.
- They form complex structures like filaments, rings, and cages through hetero-oligomerization.
- Septin interactions involve GTPase domains and terminal extensions.
Purpose of the Study:
- To critically evaluate the significance of GTP-binding and GTP hydrolysis in septin assembly and function.
- To explore the implications of GTPase domain activity in human septin mutations.
- To discuss the potential of small molecules targeting septin polymerization.
Main Methods:
- This mini-review critically assesses existing literature.
- It analyzes studies involving GTPase-inactivating mutations.
- It discusses structural determinants of septin oligomer interfaces.
Main Results:
- GTP-binding is crucial for septin assembly, but the role of GTP hydrolysis remains debated.
- GTPase-inactivating mutations have not conclusively proven the necessity of GTPase activity.
- G-domains are key structural elements for septin oligomerization.
Conclusions:
- The precise role of GTP hydrolysis in septin function requires further investigation.
- G-domains represent promising targets for developing inhibitors of septin assembly.
- Future research should focus on whether inhibiting G-domain activity can predictably modulate septin function.
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