SNARE-mediated membrane fusion

@article{Chen2001SNAREmediatedMF,
  title={SNARE-mediated membrane fusion},
  author={Y. A. Chen and R. Scheller},
  journal={Nature Reviews Molecular Cell Biology},
  year={2001},
  volume={2},
  pages={98-106}
}
SNARE proteins have been proposed to mediate all intracellular membrane fusion events. There are over 30 SNARE family members in mammalian cells and each is found in a distinct subcellular compartment. It is likely that SNAREs encode aspects of membrane transport specificity but the mechanism by which this specificity is achieved remains controversial. Functional studies have provided exciting insights into how SNARE proteins interact with each other to generate the driving force needed to fuse… Expand
SNARE proteins in membrane trafficking
TLDR
An update on the recent progress on SNAREs regulating membrane fusion events, especially the more detailed fusion processes dissected by well‐developed biophysical methods and in vitro single molecule analysis approaches is provided. Expand
Regulated exocytosis and SNARE function (Review)
  • T. Söllner
  • Biology, Medicine
  • Molecular membrane biology
  • 2003
The pairing of cognate v- and t-SNAREs between two opposing lipid bilayers drives spontaneous membrane fusion and confers specificity to intracellular membrane trafficking. These fusion events areExpand
Three SNARE complexes cooperate to mediate membrane fusion
  • Y. Hua, R. Scheller
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2001
TLDR
The increase in the inhibition of fusion observed with increasing concentration of inhibitor is best fit to a function that suggests three SNARE complexes cooperate to mediate fusion of a single vesicle. Expand
The syntaxins
SUMMARY The SNARE hypothesis predicts that a family of SNAP receptors are localized to and function in diverse intracellular membrane compartments where membrane fusion processes take place.Expand
SNARE protein structure and function.
TLDR
The SNARE superfamily has become, since its discovery approximately a decade ago, the most intensively studied element of the protein machinery involved in intracellular trafficking and there is still much to learn about how the assembly and activity of this machinery is choreographed in living cells. Expand
A reduced SNARE model for membrane fusion.
TLDR
A minimal model system was developed to mimic the SNARE-protein-mediated fusion of biological membranes and displays the key characteristics of in vivo fusion events. Expand
Multiple ER–Golgi SNARE transmembrane domains are dispensable for trafficking but required for SNARE recycling
TLDR
Yeast cells in which a particular essential ER–Golgi SNARE’s transmembrane domain has been removed remain viable and devoid of forward-trafficking defects. Expand
Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins.
TLDR
Recent findings on NTDs of syntaxins, the longin domain of VAMP proteins and SNAP-23/25 homologues in yeast are highlighted. Expand
A new catch in the SNARE.
TLDR
Several recent findings now indicate that plant SNAREs might not be limited to the conventional 'housekeeping' activities commonly attributed to vesicle trafficking, and might reflect SNARE interactions with different scaffolding and structural components of the cell. Expand
Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins
TLDR
A fundamental role is demonstrated of the SM protein: to act as a stimulatory subunit of its cognate SNARE fusion machinery, enhancing fusion specificity in a reconstituted system. Expand
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TLDR
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