Discovery of a heme-binding domain in a neuronal voltage-gated potassium channel.

ABSTRACT: The EAG (ether-à-go-go) family of voltage-gated K⁺ channels are important regulators of neuronal and cardiac action potential firing (excitability) and have major roles in human diseases such as epilepsy, schizophrenia, cancer, and sudden cardiac death. A defining feature of EAG (Kv10-12) channels is a highly conserved domain on the N terminus, known as the eag domain, consisting of a Per-ARNT-Sim (PAS) domain capped by a short sequence containing an amphipathic helix (Cap domain). The PAS and Cap domains are both vital for the normal function of EAG channels. Using heme-affinity pulldown assays and proteomics of lysates from primary cortical neurons, we identified that an EAG channel, hERG3 (Kv11.3), binds to heme. In whole-cell electrophysiology experiments, we identifi

SUBMITTER: Burton MJ 

PROVIDER: S-EPMC7504924 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature