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Science 4 August 2006:
Vol. 313. no. 5787, pp. 673 - 676
DOI: 10.1126/science.1129486

Reports

N- to C-Terminal SNARE Complex Assembly Promotes Rapid Membrane Fusion

Ajaybabu V. Pobbati, Alexander Stein, Dirk Fasshauer*

Assembly of the soluble N-ethylmaleimide–sensitive factor attachment protein receptors (SNAREs) syntaxin 1, SNAP-25, and synaptobrevin 2 is thought to be the driving force for the exocytosis of synaptic vesicles. However, whereas exocytosis is triggered at a millisecond time scale, the SNARE-mediated fusion of liposomes requires hours for completion, which challenges the idea of a key role for SNAREs in the final steps of exocytosis. We found that liposome fusion was dramatically accelerated when a stabilized syntaxin/SNAP-25 acceptor complex was used. Thus, SNAREs do have the capacity to execute fusion at a speed required for neuronal secretion, demonstrating that the maintenance of acceptor complexes is a critical step in biological fusion reactions.

Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.

* To whom correspondence should be addressed. E-mail: dfassha{at}gwdg.de

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Structural and Functional Implications of Linked SNARE Motifs in SNAP25.
L. Wang, M. A. Bittner, D. Axelrod, and R. W. Holz (2008)
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Docking of Liposomes to Planar Surfaces Mediated by trans-SNARE Complexes.
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A Role for Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor Complex Dimerization during Neurosecretion.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)