The functions of Munc18-1 in regulated exocytosis

Autor:	Alan Morgan, Robert D. Burgoyne, Leo F. Ciufo, Margaret E. Graham, Mark T. W. Handley, Jeff W. Barclay
Rok vydání:	2009
Předmět:	Vesicle fusion STX1A Qa-SNARE Proteins General Neuroscience rab3 GTP-Binding Proteins Munc-18 Biology Syntaxin 1 General Biochemistry Genetics and Molecular Biology Exocytosis Synaptotagmin 1 Syntaxin 3 Cell biology Munc18 Proteins History and Philosophy of Science Mutation Syntaxin Animals Humans Protein Binding
Zdroj:	Annals of the New York Academy of Sciences. 1152
ISSN:	1749-6632
Popis:	The activation of regulated exocytosis occurs by a rise in cytosolic Ca(2+) concentration. Synaptotagmins act as the Ca(2+) sensors, whereas the machinery that allows fusion of secretory vesicles with the plasma membrane consists of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins, including syntaxin 1, SNAP-25, and VAMP. Within the pathway leading to exocytosis, there is an essential requirement for a member of the conserved Sec1/Munc18 (SM) protein family, which in neurotransmitter and neurohormone release in mammalian cells is Munc18-1. The exact role of Munc18-1 and the steps within exocytosis in which it acts have been intensively investigated. Current evidence suggests that Munc18-1 acts via distinct modes of interactions with syntaxin 1 and the other SNARE proteins and influences all of the steps leading to exocytosis, including vesicle recruitment, tethering, docking, priming, and membrane fusion.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e7ae749083cee107b17bc11623444fc https://pubmed.ncbi.nlm.nih.gov/19161378 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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