N - to C - Terminal SNARE Complex Assembly
نویسنده
چکیده
http://www.sciencemag.org/cgi/content/full/313/5787/673 version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/cgi/content/full/313/5787/673/DC1 can be found at: Supporting Online Material found at: can be related to this article A list of selected additional articles on the Science Web sites http://www.sciencemag.org/cgi/content/full/313/5787/673#related-content http://www.sciencemag.org/cgi/content/full/313/5787/673#otherarticles , 8 of which can be accessed for free: cites 24 articles This article 29 article(s) on the ISI Web of Science. cited by This article has been http://www.sciencemag.org/cgi/content/full/313/5787/673#otherarticles 7 articles hosted by HighWire Press; see: cited by This article has been http://www.sciencemag.org/cgi/collection/cell_biol Cell Biology : subject collections This article appears in the following
منابع مشابه
Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles.
During exocytosis a four-helical coiled coil is formed between the three SNARE proteins syntaxin, synaptobrevin and SNAP-25, bridging vesicle and plasma membrane. We have investigated the assembly pathway of this complex by interfering with the stability of the hydrophobic interaction layers holding the complex together. Mutations in the C-terminal end affected fusion triggering in vivo and led...
متن کاملMunc18-1-regulated stage-wise SNARE assembly underlying synaptic exocytosis
Synaptic-soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins couple their stage-wise folding/assembly to rapid exocytosis of neurotransmitters in a Munc18-1-dependent manner. The functions of the different assembly stages in exocytosis and the role of Munc18-1 in SNARE assembly are not well understood. Using optical tweezers, we observed four distinct stages of assemb...
متن کاملThe N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly.
The SNAREs syntaxin 7, syntaxin 8, vti1b, and endobrevin/VAMP8 function in the fusion of late endosomes. Although the core complex formed by these SNAREs is very similar to the neuronal SNARE complex, it differs from the neuronal complex in that three of the four SNAREs contain extended N-terminal regions of unknown structure and function. Here we show that the N-terminal regions of syntaxin 7,...
متن کاملA transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly.
The SNARE proteins syntaxin, SNAP-25, and synaptobrevin play a central role during Ca(2+)-dependent exocytosis at the nerve terminal. Whereas syntaxin and SNAP-25 are located in the plasma membrane, synaptobrevin resides in the membrane of synaptic vesicles. It is thought that gradual assembly of these proteins into a membrane-bridging ternary SNARE complex ultimately leads to membrane fusion. ...
متن کاملIdentification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly.
Assembly of the three neuronal membrane proteins synaptobrevin, syntaxin, and SNAP-25 is thought to be one of the key steps in mediating exocytosis of synaptic vesicles. In vivo and in vitro, these proteins form a tight complex. Assembly is associated with a large increase in alpha-helical content, suggesting that major structural and conformational changes are associated with the assembly reac...
متن کاملSynaptobrevin N-terminally bound to syntaxin–SNAP-25 defines the primed vesicle state in regulated exocytosis
Rapid neurotransmitter release depends on the ability to arrest the SNAP receptor (SNARE)-dependent exocytosis pathway at an intermediate "cocked" state, from which fusion can be triggered by Ca(2+). It is not clear whether this state includes assembly of synaptobrevin (the vesicle membrane SNARE) to the syntaxin-SNAP-25 (target membrane SNAREs) acceptor complex or whether the reaction is arres...
متن کامل