期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 1, 页码 100-105出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1413764111
关键词
Vibrio parahaemolyticus; SNARE; vesicle fusion; yeast vacuole; vp1680
资金
- National Institute of Allergy and Infectious Diseases (NIAID) [R01-AI056404, R01-AI087808]
- Welch Foundation [I-1561]
- University of Georgia Startup Funds
- NIAID [R01-AI100913]
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 V-o 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 angstrom 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.
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