Article
- The EMBO Journal (2004) 23, 3483 - 3491
- doi:10.1038/sj.emboj.7600355
Published online: 19 August 2004
Subject Categories:
The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature
Yumi Yoshida1,2,a, Masahiro Kinuta1,a, Tadashi Abe1, Shuang Liang1, Kenta Araki1,2, Ottavio Cremona3, Gilbert Di Paolo4, Yoshinori Moriyama2, Tatsuji Yasuda5, Pietro De Camilli4 and Kohji Takei1
- Department of Neuroscience, Okayama University Graduate School of Medicine and Dentistry, Okayama, Japan
- Department of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University, Okayama, Japan
- DIBIT-Scientific Institute San Raffaele Universita' Vita – Salute San Raffaele, Milano, Italy
- Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT, USA
- Department of Cell Chemistry, Okayama University Graduate School of Medicine and Dentistry, Okayama, Japan
Correspondence to:
Kohji Takei, Department of Neuroscience, Okayama University Graduate School of Medicine and Dentistry, 2-5-1 Shikata-cho, Okayama 700-8558, Japan. Tel.: +81 86 235 7120; Fax: +81 86 235 7126; E-mail: kohji@md.okayama-u.ac.jp
aThese authors contributed equally to this paper
Received 5 April 2004; Accepted 14 July 2004
Abstract
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.
Keywords:
- amphiphysin,
- dynamin,
- endocytosis,
- GTPase,
- liposome
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