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Clathrin interacts specifically with amphiphysin and is displaced by dynamin.

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

Authors

  • McMahon HT
  • Wigge P
  • Smith C

Journal

FEBS letters

Publication Data

August 18, 1997

Associated Grants

None

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