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V-ATPase activity in the TGN/EE is required for exocytosis and recycling in Arabidopsis.

Identifieur interne : 002B79 ( PubMed/Corpus ); précédent : 002B78; suivant : 002B80

V-ATPase activity in the TGN/EE is required for exocytosis and recycling in Arabidopsis.

Auteurs : Yu Luo ; Stefan Scholl ; Anett Doering ; Yi Zhang ; Niloufer G. Irani ; Simone Di Rubbo ; Lutz Neumetzler ; Praveen Krishnamoorthy ; Isabelle Van Houtte ; Evelien Mylle ; Volker Bischoff ; Samantha Vernhettes ; Johan Winne ; Ji Friml ; York-Dieter Stierhof ; Karin Schumacher ; Staffan Persson ; Eugenia Russinova

Source :

RBID : pubmed:27250258

Abstract

In plants, vacuolar H(+)-ATPase (V-ATPase) activity acidifies both the trans-Golgi network/early endosome (TGN/EE) and the vacuole. This dual V-ATPase function has impeded our understanding of how the pH homeostasis within the plant TGN/EE controls exo- and endocytosis. Here, we show that the weak V-ATPase mutant deetiolated3 (det3) displayed a pH increase in the TGN/EE, but not in the vacuole, strongly impairing secretion and recycling of the brassinosteroid receptor and the cellulose synthase complexes to the plasma membrane, in contrast to mutants lacking tonoplast-localized V-ATPase activity only. The brassinosteroid insensitivity and the cellulose deficiency defects in det3 were tightly correlated with reduced Golgi and TGN/EE motility. Thus, our results provide strong evidence that acidification of the TGN/EE, but not of the vacuole, is indispensable for functional secretion and recycling in plants.

DOI: 10.1038/nplants.2015.94
PubMed: 27250258

Links to Exploration step

pubmed:27250258

Le document en format XML

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<div type="abstract" xml:lang="en">In plants, vacuolar H(+)-ATPase (V-ATPase) activity acidifies both the trans-Golgi network/early endosome (TGN/EE) and the vacuole. This dual V-ATPase function has impeded our understanding of how the pH homeostasis within the plant TGN/EE controls exo- and endocytosis. Here, we show that the weak V-ATPase mutant deetiolated3 (det3) displayed a pH increase in the TGN/EE, but not in the vacuole, strongly impairing secretion and recycling of the brassinosteroid receptor and the cellulose synthase complexes to the plasma membrane, in contrast to mutants lacking tonoplast-localized V-ATPase activity only. The brassinosteroid insensitivity and the cellulose deficiency defects in det3 were tightly correlated with reduced Golgi and TGN/EE motility. Thus, our results provide strong evidence that acidification of the TGN/EE, but not of the vacuole, is indispensable for functional secretion and recycling in plants.</div>
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