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Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane
Munc18-1 plays pleiotropic roles in neurosecretion by acting as 1) a molecular chaperone of syntaxin-1, 2) a mediator of dense-core vesicle docking, and 3) a priming factor for soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion. However, how these function...
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| Главные авторы: | , , , , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
The American Society for Cell Biology
2011
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3204074/ https://ncbi.nlm.nih.gov/pubmed/21900502 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1091/mbc.E11-02-0135 |
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