Referenced in: none

Automatically associated channels: TRP , TRPV , TRPV2

Title: Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.

Authors: Pau Doñate-Macian, Manuel Bañó-Polo, Jose-Luis Vazquez-Ibar, Ismael Mingarro, Alex Perálvarez-Marín

Journal, date & volume: Biochem. Biophys. Res. Commun., 2015 Jul 3 , 462, 221-6

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/25956061

Abstract
Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disposition in biological membranes, identifying that TM1-TM4 and TM5-TM6 regions can assemble as independent folding domains. The ARD is not required for TM domain insertion in the membrane. The folding features observed for TRPV2 may be conserved and shared among other TRP channels outside the TRPV subfamily.