6533b85cfe1ef96bd12bca1a
RESEARCH PRODUCT
Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.
Pau Doñate-maciánIsmael MingarroAlex Perálvarez-marínManuel Bañó-poloJosé Luis Vázquez-ibarsubject
Models MolecularVesicle-associated membrane protein 8Protein FoldingTRPV5Protein ConformationBiophysicsTRPV Cation ChannelsBiochemistryTRPVTransient receptor potential channelAnimalsHumansProtein Structure QuaternaryMolecular BiologyIon channelTransmembrane channelsChemistryCell MembraneCell BiologyTransmembrane proteinRecombinant ProteinsAnkyrin RepeatProtein Structure TertiaryRatsHEK293 CellsBiochemistryBiophysicsAnkyrin repeatdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-07-01 | Biochemical and biophysical research communications |