Background: The functional role of the V-ATPase as a pH-sensing receptor remains unknown. Results: N-terminal peptides from the a-subunit isoforms of the V-ATPase modulate the enzymatic GEF activity of cytohesin-2. Conclusion: V-ATPase is a novel cytohesin-signaling receptor. Significance: These data reveal an evolutionarily conserved signaling process between V-ATPase, cytohesin-2, and Arfs, which is crucial for understanding the cell biological functions of these proteins. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Hosokawa, H., Dip, P. V., Merkulova, M., Bakulina, A., Zhuang, Z., Khatri, A., … Marshansky, V. (2013). The n termini of a-subunit isoforms are involved in Signaling between Vacuolar H+-ATPase (V-ATPase) and Cytohesin-2. Journal of Biological Chemistry, 288(8), 5896–5913. https://doi.org/10.1074/jbc.M112.409169
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