Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes

Anju Sreelatha, Terry L. Bennett, Emily M. Carpinone, Kevin M. O'Brien, Kamyron D. Jordan, Dara L. Burdette, Kim Orth, Vincent J. Starai

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Vesicle fusion governs many important biological processes, and imbalances in the regulation of membrane fusion can lead to a variety of diseases such as diabetes and neurological disorders. Here we show that the Vibrio parahaemolyticus effector protein VopQ is a potent inhibitor of membrane fusion based on an in vitro yeast vacuole fusion model. Previously, we demonstrated that VopQ binds to the Vo domain of the conserved V-type H+-ATPase (V-ATPase) found on acidic compartments such as the yeast vacuole. VopQ forms a nonspecific, voltage-gated membrane channel of 18 A˚ resulting in neutralization of these compartments. We now present data showing that VopQ inhibits yeast vacuole fusion. Furthermore, we identified a unique mutation in VopQ that delineates its two functions, deacidification and inhibition of membrane fusion. The use of VopQ as a membrane fusion inhibitor in this manner now provides convincing evidence that vacuole fusion occurs independently of luminal acidification in vitro.

Original languageEnglish (US)
Pages (from-to)100-105
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number1
DOIs
Publication statusPublished - Jan 6 2015

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Keywords

  • SNARE
  • Vesicle fusion
  • Vibrio parahaemolyticus
  • vp1680
  • Yeast vacuole

ASJC Scopus subject areas

  • General

Cite this

Sreelatha, A., Bennett, T. L., Carpinone, E. M., O'Brien, K. M., Jordan, K. D., Burdette, D. L., ... Starai, V. J. (2015). Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes. Proceedings of the National Academy of Sciences of the United States of America, 112(1), 100-105. https://doi.org/10.1073/pnas.1413764111