Referenced in: none

Automatically associated channels: Kv2.1 , TRP , TRPM , TRPM8 , TRPV , TRPV1

Title: Exploring structure-function relationships between TRP and Kv channels.

Authors: Jeet Kalia, Kenton J Swartz

Journal, date & volume: Sci Rep, 2013 , 3, 1523

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/23519328

Abstract
The molecular mechanisms underlying the activation of Transient Receptor Potential (TRP) ion channels are poorly understood when compared to those of the voltage-activated potassium (Kv) channels. The architectural and pharmacological similarities between the members of these two families of channels suggest that their structure-function relationships may have common features. We explored this hypothesis by replacing previously identified domains and critical structural motifs of the membrane-spanning portions of Kv2.1 with corresponding regions of two TRP channels, TRPM8 and TRPV1. Our results show that the S3b-S4 paddle motif of Kv2.1, but not other domains, can be replaced by the analogous regions of both TRP channels without abolishing voltage-activation. In contrast, replacement of portions of TRP channels with those of Kv2.1 consistently yielded non-functional channels. Taken together, these results suggest that most structural elements within TRP channels and Kv channels are not sufficiently related to allow for the creation of hybrid channels.