SNAREs — engines for membrane fusion
- R. Jahn, R. Scheller
- BiologyNature reviews. Molecular cell biology
- 1 September 2006
A fascinating picture of these robust nanomachines is emerging, which seems to be conserved and adaptable for fusion reactions as diverse as those involved in cell growth, membrane repair, cytokinesis and synaptic transmission.
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
- R B Sutton, D. Fasshauer, R. Jahn, A. Brunger
- 24 September 1998
The X-ray crystal structure of a core synaptic fusion complex containing syntaxin-1A, synaptobrevin-II and SNAP-25B reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins.
Molecular Anatomy of a Trafficking Organelle
- S. Takamori, M. Holt, R. Jahn
- 17 November 2006
Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs.
- D. Fasshauer, R B Sutton, A. Brunger, R. Jahn
- BiologyProceedings of the National Academy of Sciences…
- 22 December 1998
The main structural features of the neuronal complex are highly conserved during evolution, and it is concluded that fusion-competent SNARE complexes generally consist of four-helix bundles composed of three Q- SNAREs and one R-SNARE.
Molecular machines governing exocytosis of synaptic vesicles
- R. Jahn, D. Fasshauer
- 10 October 2012
The molecular mechanisms of calcium-dependent exocytosis of synaptic vesicles mediates the release of neurotransmitters are surveyed in an attempt to functionally integrate the key proteins into the emerging picture of the neuronal fusion machine.
Helical extension of the neuronal SNARE complex into the membrane
The results suggest that the final phase of SNARE assembly is directly coupled to membrane merger, and this structure shows that assembly proceeds beyond the already known core SNARE complex, resulting in a continuous helical bundle that is further stabilized by side-chain interactions in the linker region.
SNAREs are concentrated in cholesterol‐dependent clusters that define docking and fusion sites for exocytosis
In the plasmalemma, syntaxins are concentrated in 200 nm large, cholesterol‐dependent clusters at which secretory vesicles preferentially dock and fuse, which suggests that high local concentrations of SNAREs are required for efficient fusion.
Structure and Conformational Changes in NSF and Its Membrane Receptor Complexes Visualized by Quick-Freeze/Deep-Etch Electron Microscopy
- P. Hanson, Robyn Roth, H. Morisaki, R. Jahn, J. Heuser
- 8 August 1997
Membrane fusion and exocytosis.
Fusion of intracellular membranes in eukaryotic cells involves several protein families including SNAREs, Rab proteins, and Sec1/Munc-18 related proteins (SM-proteins).