The n termini of a-subunit isoforms are involved in Signaling between Vacuolar H+-ATPase (V-ATPase) and Cytohesin-2

34Citations
Citations of this article
39Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free