TRPV1 temperature activation is specifically sensitive to strong decreases in amino acid hydrophobicity.

ABSTRACT: Several transient receptor potential (TRP) ion channels can be directly activated by hot or cold temperature with high sensitivity. However, the structures and molecular mechanism giving rise to their high temperature sensitivity are not fully understood. One hypothesized mechanism assumes that temperature activation is driven by the exposure of hydrophobic residues to solvent. This mechanism further predicts that residues are exposed to solvent in a coordinated fashion, but without necessarily being located in close proximity to each other. However, there is little experimental evidence supporting this mechanism in TRP channels. Here, we combined high-throughput mutagenesis, functional screening, and deep sequencing to identify mutations from a total of ~7,300 TRPV1 random mutant clones.

SUBMITTER: Sosa-Pagan JO 

PROVIDER: S-EPMC5428820 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature