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Updated: May 25, 2026

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
Published on: December 31, 2013
Interaction of transient receptor potential vanilloid 4 with annexin A2 and tubulin beta 5
Juan Huai1, Yang Zhang, Qing-Mei Liu
1Department of Physical Medicine & Rehabilitation, Qilu Hospital, Shandong University, Jinan 250012, China.
Abstract:
The aim of the present study was to investigate if there exists an interaction of TRPV4 with annexin A2 and with tubulin beta 5 in transfected human embryonic kidney (HEK293) cells in vitro. Coimmunoprecipitation of the rat dorsal root ganglion was performed to validly conform the interaction of TRPV4 with the other two proteins. Gene fragments coding for the amino acids in protein were obtained. We conducted coimmunoprecipitation and immunofluorescence on the transfected cell samples. Coimmunoprecipitation experiments of transfected HEK293 cells revealed that TRPV4 and tubulin beta 5 associated together in a complex, whereas TRPV4 and annexin A2 did not. The immunofluorescence microscopy revealed a colocalization of TRPV4 with both the tubulin beta 5 and annexin A2. These results indicate an interaction between TRPV4 and tubulin beta 5 by associating together. However, the association between TRPV4 and annexin A2 may be mediated by some intermediate elements or just exists in some physiological conditions. Thus, TRPV4 channel function may be modulated by tubulin beta 5 and annexin A2 and their interactions may play a role in the mechanosensation in the pathogenesis of neuropathic pain.
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