Topological restriction of SNARE-dependent membrane fusion

Article Abstract:

Research is presented concerning the effect which the anchoring arrangement of four-helix bundles has on the mediation of fusion in transport vehicles with target membranes within cells.

author: Sollner, Thomas H., Rothman, James E., McNew, James A., Parlati, Francesco, Fukuda, Ryouichi, Miller, Rebecca
Biochemistry, Cell membranes, Letter to the Editor

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SNAP receptors implicated in vesicle targeting and fusion

Article Abstract:

N-ethylmaleimide-sensitive fusion protein (NSF) is a membrane fusion protein which interacts with soluble NSF attachment proteins (SNAPs) during vesicle fusion. Since SNAPs bind to specific sites in membranes,an investigation was conducted to isolate and characterize SNAP receptors. Crude membrane fraction analysis identifed syntaxin, synaptobrevin and a hydrophilic SNAP-25 as SNAP receptors. It is proposed that these SNAP receptorscomprise part of a family of compartment-specific membrane proteins which function in the formation of correct vesicle-membrane attachments during fusion.

author: Brunner, Michael, Rothman, James E., Sollner, Thomas, Whiteheart, Sidney W., Erdjument-Bromage, Hediye, Geromanos, Scott, Tempst, Paul
Identification and classification, Biological transport, Cell receptors

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A possible docking and fusion particle for synaptic transmission

Article Abstract:

The soluble N-ethylmaleimide-sensitive fusion (NSF) protein, alpha-soluble NSF attachment protein (SNAP) and beta-SNAP assemble to form a docking and fusion complex for synaptic transmission. Beta-SNAP binds to synaptotagmin and recruits NSF but alpha-SNAP is unable to do so. The complex probably associates the process of membrane fusion to the entry of calcium by attaching the fusion protein, beta-SNAP, to the calcium sensor, synaptotagmin.

author: Sollner, Thomas H., Rothman, James E., Schiavo, Giampietro, Gmachl, Michael J.S., Stenbeck, Gudrun
Observations, Biosensors, Neural transmission, Synaptic transmission

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subjects list: Research, Membrane proteins, Membrane fusion
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