Human TRPA1 is an inherently mechanosensitive bilayer-gated ion channel

Lavanya Moparthi; Peter M Zygmunt

doi:10.1016/j.ceca.2020.102255

Human TRPA1 is an inherently mechanosensitive bilayer-gated ion channel

Cell Calcium. 2020 Nov:91:102255. doi: 10.1016/j.ceca.2020.102255. Epub 2020 Jul 18.

Authors

Lavanya Moparthi¹, Peter M Zygmunt²

Affiliations

¹ Wallenberg 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. Electronic address: lavanya.moparthi@liu.se.
² Department of Clinical Sciences Malmö, Lund University, SE-214 28, Malmö, Sweden. Electronic address: peter.zygmunt@med.lu.se.

PMID: 32717533
DOI: 10.1016/j.ceca.2020.102255

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.

Keywords: Mechanosensation; Mechanosensitive channel; Redox sensitivity; TRP channel; TRPA1.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Humans
Ion Channel Gating*
Lipid Bilayers / metabolism*
Mechanotransduction, Cellular*
TRPA1 Cation Channel / chemistry
TRPA1 Cation Channel / metabolism*

Substances

Lipid Bilayers
TRPA1 Cation Channel
TRPA1 protein, human