Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion

Christopher Peters, Martin J. Bayer, Susanne Bühler, Jens S. Andersen, Matthias Mann and Andreas Mayer ()
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Christopher Peters: Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft
Martin J. Bayer: Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft
Susanne Bühler: Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft
Jens S. Andersen: University of Southern Denmark, Campusvej 55
Matthias Mann: University of Southern Denmark, Campusvej 55
Andreas Mayer: Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft

Nature, 2001, vol. 409, issue 6820, 581-588

Abstract: Abstract SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) and Rab-GTPases, together with their cofactors, mediate the attachment step in the membrane fusion of vesicles. But how bilayer mixing—the subsequent core process of fusion—is catalysed remains unclear. Ca2+/calmodulin controls this terminal process in many intracellular fusion events. Here we identify V0, the membrane-integral sector of the vacuolar H+-ATPase, as a target of calmodulin on yeast vacuoles. Between docking and bilayer fusion, V0 sectors from opposing membranes form complexes. V0 trans-complex formation occurs downstream from trans-SNARE pairing, and depends on both the Rab-GTPase Ypt7 and calmodulin. The maintenance of existing complexes and completion of fusion are independent of trans-SNARE pairs. Reconstituted proteolipids form sealed channels, which can expand to form aqueous pores in a Ca2+/calmodulin-dependent fashion. V0 trans-complexes may therefore form a continuous, proteolipid-lined channel at the fusion site. We propose that radial expansion of such a protein pore may be a mechanism for intracellular membrane fusion.

Date: 2001
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DOI: 10.1038/35054500

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