Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Endophilin/SH3p4 is a protein highly enriched in nerve terminals that binds the GTPase dynamin and the polyphosphoinositide phosphatase synaptojanin, two proteins implicated in synaptic vesicle endocytosis. We show here that antibody-mediated disruption of endophilin function in a tonically stimulated synapse leads to a block in the invagination of clathrin-coated pits adjacent to the active zone and therefore to a block of synaptic vesicle recycling. We also show that in a cell-free system, endophilin is not associated with clathrin coats and is a functional partner of dynamin. Our findings suggest that endophilin is part of a biochemical machinery that acts in trans to the clathrin coat from early stages to vesicle fission.
Язык оригинала | английский |
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Страницы (с-по) | 143-154 |
Число страниц | 12 |
Журнал | Neuron |
Том | 24 |
Номер выпуска | 1 |
DOI | |
Состояние | Опубликовано - 1 янв 1999 |
Опубликовано для внешнего пользования | Да |
ID: 40835098