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Dynamin and its role in membrane fission
1Laboratory of Cell Biochemistry and Biology, National Institutes of Health, Bethesda, Maryland 20892, USA. jennyh@helix.nih.gov
Annual Review of Cell and Developmental Biology
|October 14, 2000
Summary
Dynamin, a GTPase, is crucial for vesicle formation and membrane fission. Its self-assembly into rings or spirals explains its role in endocytosis and cellular trafficking.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Dynamin is a 100-kDa GTPase vital for endocytosis, synaptic vesicle recycling, and Golgi trafficking.
- It possesses a GTPase domain, a PH domain for membrane binding, a GED for self-assembly, and a PRD for partner interactions.
Purpose of the Study:
- To review the relationship between dynamin's GTPase and self-assembly properties.
- To elucidate dynamin's role in cellular functions like vesicle formation and membrane fission.
Main Methods:
- Literature review focusing on dynamin's biochemical and structural properties.
- Analysis of existing data on dynamin's GTPase activity, self-assembly, and interactions with binding partners.
Main Results:
- Dynamin self-assembles into rings or spirals, supporting its proposed role in wrapping and constricting vesicle necks.
- Dynamin's GTPase activity is stimulated by self-assembly and interactions with binding partners via the PRD.
Conclusions:
- Dynamin's ability to self-assemble is intrinsically linked to its GTPase function and essential for membrane fission during endocytosis.
- Understanding these properties provides insight into dynamin's critical role in diverse cellular membrane dynamics.