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Article
The Angiotensin II Type 1 Receptor C-Terminal Lys Residues Interact with Tubulin and Modulate Receptor Export Trafficking
PLoS ONE
  • Xiaoping Zhang
  • Hong Wang
  • Matthew T. Duvernay
  • Shu Zhu, Philadelphia College of Osteopathic Medicine
  • Guangyu Wu
Document Type
Article
Publication Date
1-1-2013
Abstract
The physiological and pathological functions of angiotensin II are largely mediated through activating the cell surface angiotensin II type 1 receptor (AT1R). However, the molecular mechanisms underlying the transport of newly synthesized AT1R from the endoplasmic reticulum (ER) to the cell surface remain poorly defined. Here we demonstrated that the C-terminus (CT) of AT1R directly and strongly bound to tubulin and the binding domains were mapped to two consecutive Lys residues at positions 310 and 311 in the CT membrane-proximal region of AT1R and the acidic CT of tubulin, suggestive of essentially ionic interactions between AT1R and tubulin. Furthermore, mutation to disrupt tubulin binding dramatically inhibited the cell surface expression of AT1R, arrested AT1R in the ER, and attenuated AT1R-mediated signaling measured as ERK1/2 activation. These data demonstrate for the first time that specific Lys residues in the CT juxtamembrane region regulate the processing of AT1R through interacting with tubulin. These data also suggest an important role of the microtubule network in the cell surface transport of AT1R. © 2013 Zhang et al.
Comments

This article was published in PLoS ONE, Volume 8, Issue 2.

The published version is available at http://dx.doi.org/10.1371/journal.pone.0057805.

Copyright © 2013 Scopus.

Citation Information
Xiaoping Zhang, Hong Wang, Matthew T. Duvernay, Shu Zhu, et al.. "The Angiotensin II Type 1 Receptor C-Terminal Lys Residues Interact with Tubulin and Modulate Receptor Export Trafficking" PLoS ONE Vol. 8 Iss. 2 (2013)
Available at: http://works.bepress.com/shu_zhu/8/