The vesicular ATPase: a missing link between acidification and exocytosis

Dong Wang, P Robin Hiesinger, Dong Wang, P Robin Hiesinger

Abstract

The vesicular adenosine triphosphatase (ATPase) acidifies intracellular compartments, including synaptic vesicles and secretory granules. A controversy about a second function of this ATPase in exocytosis has been fuelled by questions about multiple putative roles of acidification in the exocytic process. Now, Poëa-Guyon et al. (2013. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201303104) present new evidence that the vesicular ATPase performs separate acidification and exocytosis roles and propose a mechanism for how these two functions are causally linked.

Figures

Figure 1.
Figure 1.
V-ATPase V0–V1 association blocks secretion. (A) Poëa-Guyon et al. (2013) suggest that dissociation of V0 (red boxes) and V1 (green cylinders) sectors follows vesicle acidification (yellow) and frees the V0 sector for an acute, acidification-independent function in secretion.(B) V-ATPase–independent pharmacological disruption of vesicular acidification causes increased V0–V1 assembly of the functional proton pump, which in turn blocks secretion.(C) Pharmacological disruption of the V-ATPase disrupts both vesicle acidification and V0–V1 assembly, thereby permitting V0-dependent secretion. This mechanism can override disruption of acidification shown in B and restores secretion of nonacidified vesicles.

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