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Clathrin interacts specifically with amphiphysin and is displaced by dynamin.

FEBS letters | Aug 18, 1997

http://www.ncbi.nlm.nih.gov/pubmed/9280305

Amphiphysin is an SH3 domain protein that has been implicated in synaptic vesicle endocytosis. We have recently cloned a second amphiphysin isoform, Amph2 (sequence submitted to GenBank, Y13380). Proteins capable of forming a complex with amphiphysin were isolated from rat brain by using recombinant GST-Amph2 for binding experiments. As well as interacting with dynamin I, the full-length protein bound to a weaker 180-kDa band. Immunoblotting demonstrated this protein to be clathrin. To address whether this is a direct interaction, the clathrin binding to amphiphysin was reconstituted in vitro with purified proteins. The N-terminal domain of Amph2 is sufficient for clathrin binding. Dynamin, which interacts with the SH3 domain of Amph2, displaces clathrin from the N-terminus. We propose a model that may explain how clathrin and dynamin are recruited to non-overlapping sites of the coated pit.

Pubmed ID: 9280305 RIS Download

Mesh terms: Adaptor Protein Complex alpha Subunits | Adaptor Proteins, Vesicular Transport | Animals | Brain | Cell Extracts | Clathrin | Dynamin I | Dynamins | GTP Phosphohydrolases | Membrane Proteins | Molecular Sequence Data | Nerve Tissue Proteins | Protein Binding | Rats | Recombinant Fusion Proteins | Swine

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Mouse Genome Informatics (Data, Gene Annotation)

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