Gating and regulation of KCNH (ERG, EAG, and ELK) channels by intracellular domains
MetadataShow full item record
AbstractThe KCNH family comprises the ERG, EAG, and ELK voltage-activated, potassium-selective channels. Distinct from other K channels, KCNH channels contain unique structural domains, including a PAS (Per-Arnt-Sim) domain in the N-terminal region and a CNBHD (cyclic nucleotide-binding homology domain) in the C-terminal region. The intracellular PAS domains and CNBHDs interact directly and regulate some of the characteristic gating properties of each type of KCNH channel. The PAS-CNBHD interaction regulates slow closing (deactivation) of hERG channels, the kinetics of activation and pre-pulse dependent population of closed states (the Cole-Moore shift) in EAG channels and voltage-dependent potentiation in ELK channels. KCNH channels are all regulated by an intrinsic ligand motif in the C-terminal region which binds to the CNBHD. Here, we focus on some recent advances regarding the PAS-CNBHD interaction and the intrinsic ligand.
KeywordCNBHD cyclic nucleotide-binding domain
EAG K channel
ELK K channel
Identifier to cite or link to this itemhttp://hdl.handle.net/10713/13747
- The structural mechanism of KCNH-channel regulation by the eag domain.
- Authors: Haitin Y, Carlson AE, Zagotta WN
- Issue date: 2013 Sep 19
- Structure of the carboxy-terminal region of a KCNH channel.
- Authors: Brelidze TI, Carlson AE, Sankaran B, Zagotta WN
- Issue date: 2012 Jan 9
- Dynamic rearrangement of the intrinsic ligand regulates KCNH potassium channels.
- Authors: Dai G, James ZM, Zagotta WN
- Issue date: 2018 Apr 2
- Direct interaction of eag domains and cyclic nucleotide-binding homology domains regulate deactivation gating in hERG channels.
- Authors: Gianulis EC, Liu Q, Trudeau MC
- Issue date: 2013 Oct
- The hERG potassium channel intrinsic ligand regulates N- and C-terminal interactions and channel closure.
- Authors: Codding SJ, Trudeau MC
- Issue date: 2019 Apr 1