Journal
EMBO JOURNAL
Volume 23, Issue 17, Pages 3483-3491Publisher
WILEY
DOI: 10.1038/sj.emboj.7600355
Keywords
amphiphysin; dynamin; endocytosis; GTPase; liposome
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Funding
- Fondazione Telethon Funding Source: Custom
- NCI NIH HHS [CA46128, P01 CA046128] Funding Source: Medline
- NINDS NIH HHS [R01 NS036251, R37 NS036251, NS 36251] Funding Source: Medline
- Telethon [D.111] Funding Source: Medline
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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.
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