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Dynamin spirals
1Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. jennyh@helix.nih.gov
Current Opinion in Structural Biology
|May 14, 1999
Summary
Dynamin protein is crucial for membrane recycling and cellular processes. New research shows dynamin can form structures that pinch off vesicles, suggesting its role in endocytosis.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Dynamin is recognized for its role in membrane recycling within cells.
- Its function in clathrin-mediated endocytosis is supported by various assays and structural studies.
- Previous research focused on dynamin's assembled spiral structure.
Purpose of the Study:
- To investigate the direct mechanism of dynamin in vesicle formation.
- To explore dynamin's capability to induce membrane scission independently.
- To provide evidence for dynamin's direct role in the final step of endocytosis.
Main Methods:
- Liposome binding assays to study dynamin-membrane interactions.
- In vitro reconstitution of dynamin-mediated membrane constriction and vesiculation.
- Biochemical analysis of dynamin's GTPase activity in relation to membrane dynamics.
Main Results:
- Dynamin binds to liposomes and self-assembles into helical structures.
- GTP addition leads to the constriction and vesiculation of these dynamin-liposome tubes.
- These findings demonstrate dynamin's intrinsic ability to mediate membrane fission.
Conclusions:
- Dynamin possesses the inherent capability to drive membrane scission.
- The observed in vitro behavior strongly suggests dynamin's direct role in pinching off vesicles during endocytosis.
- Dynamin is a key mechanical component responsible for vesicle formation at the plasma membrane.