ArticleEuropean biophysics journal : EBJ2009
Roles of surface residues of intracellular domains of heag potassium channels.
Article in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- The EAG Voltage-Dependent KFrontiers in pharmacology · 2020Review
- Eag1 Voltage-Dependent Potassium Channels: Structure, Electrophysiological Characteristics, and Function in Cancer.The Journal of membrane biology · 2017Review
- The intrinsically liganded cyclic nucleotide-binding homology domain promotes KCNH channel activation.The Journal of general physiology · 2017Article
- Alternatively Spliced Isoforms of KV10.1 Potassium Channels Modulate Channel Properties and Can Activate Cyclin-dependent Kinase in Xenopus Oocytes.The Journal of biological chemistry · 2015Article
- The enigmatic cytoplasmic regions of KCNH channels.Journal of molecular biology · 2015Review
- The subfamily-specific assembly of Eag and Erg K+ channels is determined by both the amino and the carboxyl recognition domains.The Journal of biological chemistry · 2014Article
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- Article
- Structure of the C-terminal region of an ERG channel and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cysteines control the N- and C-linker-dependent gating of KCNH1 potassium channels.Biochimica et biophysica acta · 2012Article
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- Cytoplasmic domains and voltage-dependent potassium channel gating.Frontiers in pharmacology · 2012Article
- 14-3-3θ is a binding partner of rat Eag1 potassium channels.PloS one · 2012Article
- Intracellular linkers are involved in Mg2+-dependent modulation of the Eag potassium channel.Channels (Austin, Tex.)Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ether-a-go-go potassium channels have large intracellular regions containing 'Per-Ant-Sim' (PAS) and cyclic nucleotide binding (cNBD) domains at the N- and C-termini, respectively. In heag1 and heag2 channels, recent studies have suggested that the N- and C-terminal domains interact, and affect activation properties. Here, we have studied the effect of mutations of residues on the surfaces of PAS and cNBD domains. For this, we introduced alanine and lysine mutations in heag1 channels, and recorded currents by two-electrode voltage clamp. In both the PAS domain and the cNBD domain, contiguous areas of conserved residues on the surfaces of these domains were found which affected the activation kinetics of the channel. Next, we investigated possible effects of mutations on domain interactions of PAS and cNBD proteins in heag2 by co-expressing these domain proteins followed by analysis with native gels and western blotting. We found oligomeric association between these domains. Mutations F30A and A609K (on the surfaces of the PAS and cNBD domains, respectively) affected oligomeric compositions of these domains when proteins for PAS and cNBD domains were expressed together. Taken together, the data suggest that the PAS and cNBD domains form interacting oligomers that have roles in channel function.
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