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The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature
Author(s) -
Yoshida Yumi,
Kinuta Masahiro,
Abe Tadashi,
Liang Shuang,
Araki Kenta,
Cremona Ottavio,
Di Paolo Gilbert,
Moriyama Yoshinori,
Yasuda Tatsuji,
De Camilli Pietro,
Takei Kohji
Publication year - 2004
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600355
Subject(s) - amphiphysin , dynamin , liposome , endocytosis , endocytic cycle , chemistry , gtpase , microbiology and biotechnology , biophysics , internalization , synaptic vesicle recycling , vesicle , cytosol , biochemistry , synaptic vesicle , biology , membrane , receptor , enzyme
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.