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Updated: Dec 13, 2025

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4
Published on: December 31, 2013
Human TRPA1 is an inherently mechanosensitive bilayer-gated ion channel
Lavanya Moparthi1, Peter M Zygmunt2
1Wallenberg Centre for Molecular Medicine, Linköping University, SE-581 83, Linköping, Sweden; Department of Biomedical and Clinical Sciences (BKV), Faculty of Health Sciences, Linköping University, SE-581 83, Linköping, Sweden.
Abstract:
The role of mammalian Transient Receptor Potential Ankyrin 1 (TRPA1) as a mechanosensor is controversial. Here, we report that purified human TRPA1 (hTRPA1) with and without its N-terminal ankyrin repeat domain responded with pressure-dependent single-channel current activity when reconstituted into artificial lipid bilayers. The hTRPA1 activity was abolished by the thiol reducing agent TCEP. Thus, depending on its redox state, hTRPA1 is an inherent mechanosensitive ion channel gated by force-from-lipids.
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