The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature

Yumi Yoshida, Masahiro Kinuta, Tadashi Abe, Shuang Liang, Kenta Araki, Ottavio Cremona, Gilbert Di Paolo, Yoshinori Moriyama, Tatsuji Yasuda, Pietro De Camilli, Kohji Takei

Research output: Contribution to journalArticlepeer-review

97 Citations (Scopus)


Amphiphysin is a major dynamin-binding partner at the synapse; however, its function in fission is unclear. Incubation of large unilamellar liposomes with mice brain cytosol led to massive formation of small vesicles, whereas cytosol of amphiphysin 1 knockout mice was much less efficient in this reaction. Vesicle formation from large liposomes by purified dynamin was also strongly enhanced by amphiphysin. In the presence of liposomes, amphiphysin strongly affected dynamin GTPase activity and the recruitment of dynamin to the liposomes, but this activity was highly dependent on liposome size. Deletion from amphiphysin of its central proline-rich stretch dramatically potentiated its effect on dynamin, possibly by relieving an inhibitory intramolecular interaction. These results suggest a model in which maturation of endocytic pits correlates with the oligomerization of dynamin with either amphiphysin or other proteins with similar domain structure. Formation of these complexes is coupled to the activation of dynamin GTPase activity, thus explaining how deep invagination of the pit leads to fission.

Original languageEnglish
Pages (from-to)3483-3491
Number of pages9
JournalEMBO Journal
Issue number17
Publication statusPublished - Sept 1 2004


  • Amphiphysin
  • Dynamin
  • Endocytosis
  • GTPase
  • Liposome

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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