Cellular and functional insights into FIH-mediated hydroxylation of TRPA1.

ABSTRACT: Transient receptor potential cation channel, subfamily A, member 1 (TRPA1), also known as transient receptor potential ankyrin 1, is an ion channel located on the plasma membrane of cells. It is best known as a sensor for pain, cold, and itch in humans and other mammals, as well as for detecting electrophilic sensory irritants, including allyl isothiocyanate. A previous study confirmed that TRPA1 undergoes hydroxylation at Asn336, catalyzed by the 2-oxoglutarate oxygenase factor-inhibiting hypoxia-inducible factor (FIH). However, the biological significance of this modification remains unclear. Here, we present cellular and functional studies on the consequences of FIH-mediated asparaginyl hydroxylation of TRPA1. Coimmunoprecipitation experiments indicate that TRPA1 interacts with FIH in c

SUBMITTER: Guo T 

PROVIDER: S-EPMC12719648 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature