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Docking of Liposomes to Planar Surfaces Mediated by trans-SNARE Complexes

Olga Vites ^*, Ernst-Ludwig Florin ^*  and Reinhard Jahn ^*

^* Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany; Center for Nonlinear Dynamics, Department of Physics, University of Texas, Austin, Texas

Correspondence: Address reprint requests to Reinhard Jahn, Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 37077, Göttingen, Germany. Tel.: 49-551-201-1635; Fax: 49-551-201-1639; E-mail: rjahn{at}gwdg.de.

Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) play a key role in membrane fusion in the secretory pathway. In vitro, SNAREs spontaneously assemble into helical SNARE complexes with the transmembrane domains at the C-terminal end. During fusion, SNAREs are thought to bridge the two membranes and assemble in a zipper-like fashion, pulling the membranes together and initiating fusion. However, it is not clear to what extent SNARE assembly contributes to membrane attachment and membrane fusion. Using the neuronal SNAREs synaptobrevin (VAMP), SNAP-25, and syntaxin as examples, we show here that liposomes containing synaptobrevin firmly attach to planar surfaces containing immobilized syntaxin. Attachment requires the formation of SNARE complexes because it is dependent on the presence of SNAP-25. Binding is competed for by soluble SNARE fragments, with noncognate SNAREs such as endobrevin (VAMP8), VAMP4, and VAMP7 (Ti-VAMP) being effective but less potent in some cases. Furthermore, although SNAP-23 is unable to substitute for SNAP-25 in the attachment assay, it forms complexes of comparable stability and is capable of substituting in liposome fusion assays. Vesicle attachment is initiated by SNARE assembly at the N-terminal end of the helix bundle. We conclude that SNAREs can indeed form stable trans-complexes that result in vesicle attachment if progression to fusion is prevented, further supporting the zipper model of SNARE function.