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Clathrin interacts specifically with amphiphysin and is displaced by dynamin
H T McMahon1, P Wigge, C Smith
1Neurobiology Division, MRC-LMB, Cambridge, UK. hmm@mrc-lmb.cam.ac.uk
FEBS Letters
|August 18, 1997
Summary
Researchers identified a new amphiphysin isoform, Amph2, which binds to clathrin. Dynamin I interacts with Amph2
Area of Science:
- Molecular Biology
- Cell Biology
- Neuroscience
Background:
- Amphiphysin is a key protein in synaptic vesicle endocytosis.
- A second amphiphysin isoform, Amph2, has been identified.
Purpose of the Study:
- To investigate the binding interactions of Amph2.
- To elucidate the roles of amphiphysin isoforms in endocytosis.
Main Methods:
- Protein binding experiments using recombinant GST-Amph2.
- Co-immunoprecipitation and immunoblotting.
- In vitro reconstitution of protein interactions.
Main Results:
- Amph2 interacts with both dynamin I and clathrin.
- The N-terminal domain of Amph2 mediates clathrin binding.
- Dynamin I binding to the SH3 domain of Amph2 displaces clathrin.
Conclusions:
- A model is proposed for the recruitment of clathrin and dynamin to coated pits.
- Amphiphysin isoforms play distinct roles in synaptic vesicle endocytosis.