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V-ATPase: a potential pH sensor

Nature Cell Biology volume 8, pages 107–109 (2006)Cite this article

An interaction between V-ATPase, a multi-subunit complex responsible for endosome acidification, and ARNO, the GDP/GTP exchange factor for ARF1 and ARF6, indicates that V-ATPase is the long-sought pH-sensor that regulates trafficking in the endocytic pathway.

Endocytosis is responsible for internalizing extracellular fluid and macromolecules, as well as plasma membrane proteins, receptors and their bound ligands. While most internalized surface molecules are recycled, many endocytosed ligands dissociate from their receptors because of the low endosomal pH and travel through endosomal compartments for degradation1. Endosomal acidification is accomplished by vacuolar (H+)-ATPases (V-ATPases), which translocate protons across endosomal membranes2. In addition to triggering ligand–receptor dissociation, intra-endosomal acidification is also known to have an impact on transport along the endocytic pathway. A pH-sensor that may couple intra-endosomal pH to the formation of endocytic transport vesicles has been postulated, but this mechanism has remained poorly defined at the molecular level. On page 124, Hurtado-Lorenzo et al. demonstrate that the V-ATPase interacts directly with the endocytic transport machinery. In addition, through its pH-dependent interactions with the small GTP-binding protein ARF6 and its GDP/GTP exchange factor ARNO, the V-ATPase regulates transport from early to late endosomes, thus meeting the criteria expected of the proposed pH sensor3.

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Figure 1: V-ATPase-dependent regulation of endocytic trafficking.

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  1. the Membrane and Cytoskeleton Dynamics Group, UMR144 CNRS/Institut Curie, Paris, France

    Chiara Recchi & Philippe Chavrier

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  1. Chiara Recchi
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  2. Philippe Chavrier
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Recchi, C., Chavrier, P. V-ATPase: a potential pH sensor. Nat Cell Biol 8, 107–109 (2006). https://doi.org/10.1038/ncb0206-107

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