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Published 19 December 2005. doi:10.1083/jcb.200510018
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 6, 981-990
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Article

 Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion

Christoph Reese and Andreas Mayer

Département de Biochimie, Université de Lausanne, 1066 Epalinges, Switzerland

Correspondence to Andreas Mayer: Andreas.Mayer{at}unil.ch

Fusion pore opening and expansion are considered the most energy-demanding steps in viral fusion. Whether this also applies to soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor (SNARE)– and Rab-dependent fusion events has been unknown. We have addressed the problem by characterizing the effects of lysophosphatidylcholine (LPC) and other late-stage inhibitors on lipid mixing and pore opening during vacuole fusion. LPC inhibits fusion by inducing positive curvature in the bilayer and changing its biophysical properties. The LPC block reversibly prevented formation of the hemifusion intermediate that allows lipid, but not content, mixing. Transition from hemifusion to pore opening was sensitive to guanosine-5'-({gamma}-thio)triphosphate. It required the vacuolar adenosine triphosphatase V0 sector and coincided with its transformation. Pore opening was rate limiting for the reaction. As with viral fusion, opening the fusion pore may be the most energy-demanding step for intracellular, SNARE-dependent fusion reactions, suggesting that fundamental aspects of lipid mixing and pore opening are related for both systems.

Abbreviations used in this paper: ALP, alkaline phosphatase; BAPTA, 1,2-bis-(o-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid; GTP{gamma}S, guanosine-5'-({gamma}-thio)triphosphate; LPC, lysophosphatidylcholine; MED, myristoylated alanine-rich C kinase substrate effector domain peptide; Rh-PE, lissamine rhodamine B 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine.


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