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Job sharing in the endomembrane system: vacuolar acidification requires the combined activity of V-ATPase and V-PPase

The presence of a large central vacuole is one of the hallmarks of a prototypical plant cell, and the multiple functions of this compartment require massive fluxes of molecules across its limiting membrane, the tonoplast. Transport is assumed to be energized by the membrane potential and the proton...

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Main Authors: Kriegel, Anne (Author) , Andrés González, Zaida (Author) , Medzihradszky, Anna (Author) , Krüger, Falco (Author) , Scholl, Stefan (Author) , Delang, Simon (Author) , Patir, Meliha Gorkem (Author) , Pfeiffer, Anne (Author) , Krebs, Melanie (Author) , Lohmann, Jan U. (Author) , Schumacher, Karin (Author)
Format: Article (Journal)
Language:English
Published: 2015
In: The plant cell
Year: 2015, Volume: 27, Issue: 12, Pages: 3383-3396
ISSN:1532-298X
DOI:10.1105/tpc.15.00733
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1105/tpc.15.00733
Verlag, kostenfrei, Volltext: http://www.plantcell.org/content/27/12/3383
Verlag, kostenfrei, Volltext: http://www.plantcell.org/content/plantcell/27/12/3383.full.pdf
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Author Notes:Anne Kriegel, Zaida Andrés, Anna Medzihradszky, Falco Krüger, Stefan Scholl, Simon Delang, M. Görkem Patir-Nebioglu, Gezahegn Gute, Haibing Yang, Angus S. Murphy, Wendy Ann Peer, Anne Pfeiffer, Melanie Krebs, Jan U. Lohmann, Karin Schumacher

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520 |a The presence of a large central vacuole is one of the hallmarks of a prototypical plant cell, and the multiple functions of this compartment require massive fluxes of molecules across its limiting membrane, the tonoplast. Transport is assumed to be energized by the membrane potential and the proton gradient established by the combined activity of two proton pumps, the vacuolar H+-pyrophosphatase (V-PPase) and the vacuolar H+-ATPase (V-ATPase). Exactly how labor is divided between these two enzymes has remained elusive. Here, we provide evidence using gain- and loss-of-function approaches that lack of the V-ATPase cannot be compensated for by increased V-PPase activity. Moreover, we show that increased V-ATPase activity during cold acclimation requires the presence of the V-PPase. Most importantly, we demonstrate that a mutant lacking both of these proton pumps is conditionally viable and retains significant vacuolar acidification, pointing to a so far undetected contribution of the trans-Golgi network/early endosome-localized V-ATPase to vacuolar pH. 
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