Purified human TRPA1 activity is gated by force-from-lipids in artificial bilayers.
•
The TRPA1 N-terminal ankyrin repeat domain is not required for mechanosensation.
•
The TRPA1 mechanosensitivity is dependent on its redox state.
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.
