Homotypic vacuole fusion in yeast requires organelle acidification and not the V-ATPase membrane domain

Coonrod, E.M., Graham, L.A., Carpp, L.N., Carr, T.M., Stirrat, L., Bowers, K., Bryant, N.J. and Stevens, T.H. (2013) Homotypic vacuole fusion in yeast requires organelle acidification and not the V-ATPase membrane domain. Developmental Cell, 27(4), pp. 462-468.

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Abstract

Studies of homotypic vacuole-vacuole fusion in the yeast Saccharomyces cerevisiae have been instrumental in determining the cellular machinery required for eukaryotic membrane fusion and have implicated the vacuolar H+-ATPase (V-ATPase). The V-ATPase is a multisubunit, rotary proton pump whose precise role in homotypic fusion is controversial. Models formulated from in vitro studies suggest that it is the proteolipid proton-translocating pore of the V-ATPase that functions in fusion, with further studies in worms, flies, zebrafish, and mice appearing to support this model. We present two in vivo assays and use a mutant V-ATPase subunit to establish that it is the H+-translocation/vacuole acidification function, rather than the physical presence of the V-ATPase, that promotes homotypic vacuole fusion in yeast. Furthermore, we show that acidification of the yeast vacuole in the absence of the V-ATPase rescues vacuole-fusion defects. Our results clarify the in vivo requirements of acidification for membrane fusion.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Carpp, Ms Lindsay and Bryant, Dr Nia and Stirrat, Mrs Laura and Carr, Mr Thomas
Authors: Coonrod, E.M., Graham, L.A., Carpp, L.N., Carr, T.M., Stirrat, L., Bowers, K., Bryant, N.J., and Stevens, T.H.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Developmental Cell
Publisher:Cell Press
ISSN:1534-5807
ISSN (Online):1878-1551

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