Article
Interaction between the Linker, Pre-S1, and TRP Domains Determines Folding, Assembly, and Trafficking of TRPV Channels.
Structure (London, England : 1993) - 4 Aug 2015
Garcia-Elias Anna, Berna-Erro Alejandro, Rubio-Moscardo Fanny, Pardo-Pastor Carlos, Mrkonjić Sanela, Sepúlveda Romina V, Vicente Rubén, González-Nilo Fernando, Valverde Miguel A
Abstract excerpt
Functional transient receptor potential (TRP) channels result from the assembly of four subunits. Here, we show an interaction between the pre-S1, TRP, and the ankyrin repeat domain (ARD)-S1 linker domains of TRPV1 and TRPV4 that is essential for proper channel assembly. Neutralization of TRPV4 pre-S1 K462 resulted in protein retention in the ER, defective glycosylation and trafficking, and unresponsiveness to...
Topics
- Amino Acid Sequence
- Gene Expression
- HEK293 Cells
- HeLa Cells
- Humans
- Hydrogen Bonding
- Membrane Potentials
- Molecular Dynamics Simulation
- Molecular Sequence Data
- Mutation
- Protein Folding
- Protein Interaction Domains and Motifs