Electrostatic attraction at the core of membrane fusion.
SNARE proteins appear to be involved in homotypic and heterotypic membrane fusion events [Sollner et al. (1993) Nature 362, 318-324]. The crystal structure of the synaptic SNARE complex exhibits a parallel four-helical bundle fold with two helices contributed by SNAP-25, a target SNARE (t-SNARE), and the other two by a different t-SNARE, syntaxin, and a donor vesicle SNARE (v-SNARE), synaptobrevin. The carboxy-terminal boundary of the complex, predicted to occur at the closest proximity between the apposed membranes, displays a high density of positively charged residues. This feature combined with the enrichment of negatively charged phospholipids in the cytosolic exposed leaflet of the membrane bilayer suggest that electrostatic attraction between oppositely charged interfaces may be sufficient to induce dynamic and discrete micellar discontinuities of the apposed membranes with the transient breakdown at the junction and subsequent reformation. Thus, the positively charged end of the SNARE complex in concert with Ca2+ may be sufficient to generate a transient 'fusion pore'.
Montal
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Department of Biology, University of California San Diego, La Jolla 92093, USA. montal@biomail.ucsd.edu
D002118:Calcium / Q000378:metabolism; D008561:Membrane Fusion / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D010743:Phospholipids / Q000378:metabolism; D050600:SNARE Proteins; D055672:Static Electricity; D033921:Vesicular Transport Proteins
D008565:Membrane Proteins; D010743:Phospholipids; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins; D002118:Calcium