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The function of dynamin in endocytosis
P De Camilli1, K Takei, P S McPherson
1Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA. pietro-decamilli@quickmail.yale.edu
Current Opinion in Neurobiology
|October 1, 1995
Summary
Temperature-sensitive Drosophila mutants show paralysis due to impaired synaptic vesicle endocytosis. The GTPase dynamin, crucial for vesicle fission, forms rings that change conformation during GTP hydrolysis, blocking this process.
Area of Science:
- Neuroscience
- Cell Biology
- Genetics
Background:
- Temperature-sensitive mutants of Drosophila melanogaster exhibit rapid paralysis at restrictive temperatures.
- This paralysis is linked to a disruption in synaptic vesicle endocytosis.
- The shibire gene encodes dynamin, a GTPase implicated in vesicle trafficking.
Purpose of the Study:
- To investigate the role of dynamin in synaptic vesicle endocytosis.
- To understand the mechanism by which shibire mutants are paralyzed.
Main Methods:
- Utilizing temperature-sensitive shibire mutants of Drosophila melanogaster.
- Observing paralysis phenotypes upon temperature shift.
- Analyzing the role of dynamin in clathrin-coated pit dynamics.
Main Results:
- Shibire mutants display rapid paralysis at restrictive temperatures.
- A block in synaptic vesicle endocytosis is identified as the cause of paralysis.
- Dynamin forms rings at the neck of invaginated clathrin-coated pits.
Conclusions:
- Dynamin's conformational change, linked to GTP hydrolysis, is essential for vesicle fission.
- Disruption of dynamin function leads to impaired endocytosis and paralysis in Drosophila.