Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis

Nat Cell Biol. 1999 May;1(1):33-9. doi: 10.1038/9004.


Amphiphysin, a protein that is highly concentrated in nerve terminals, has been proposed to function as a linker between the clathrin coat and dynamin in the endocytosis of synaptic vesicles. Here, using a cell-free system, we provide direct morphological evidence in support of this hypothesis. Unexpectedly, we also find that amphiphysin-1, like dynamin-1, can transform spherical liposomes into narrow tubules. Moreover, amphiphysin-1 assembles with dynamin-1 into ring-like structures around the tubules and enhances the liposome-fragmenting activity of dynamin-1 in the presence of GTP. These results show that amphiphysin binds lipid bilayers, indicate a potential function for amphiphysin in the changes in bilayer curvature that accompany vesicle budding, and imply a close functional partnership between amphiphysin and dynamin in endocytosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Brain / metabolism
  • Cattle
  • Cell-Free System
  • Clathrin / chemistry
  • Clathrin / metabolism*
  • Clathrin / ultrastructure
  • Coated Pits, Cell-Membrane / physiology
  • Coated Pits, Cell-Membrane / ultrastructure
  • Dimerization
  • Dynamin I
  • Dynamins
  • Endocytosis / physiology*
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / metabolism*
  • GTP Phosphohydrolases / ultrastructure
  • Humans
  • Kinetics
  • Liposomes
  • Microscopy, Electron
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism*
  • Nerve Tissue Proteins / ultrastructure
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / ultrastructure


  • Clathrin
  • Liposomes
  • Nerve Tissue Proteins
  • Recombinant Proteins
  • amphiphysin
  • Dynamin I
  • GTP Phosphohydrolases
  • Dynamins