Clathrin interacts specifically with amphiphysin and is displaced by dynamin1
Authors:
- Harvey T McMahonHMHarvey T McMahon
- Patrick WiggePWPatrick Wigge
- Corrin SmithCSCorrin Smith
- 18 August 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 413 (2) , 319-322
Abstract
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.Keywords
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