ArticleThe Journal of biological chemistry2012
The Kv7.2/Kv7.3 heterotetramer assembles with a random subunit arrangement.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Structural basis of the neuronal M-current generated by an asymmetric KCNQ2/3 assembly.Cell research · 2026Article
- Temporal multi-omic exploration of the ventral tegmental area in chronic pain and passive coping behaviors.iScience · 2026Article
- Assessment of gabapentin efficacy in patients with KCNQ2-developmental epileptic encephalopathy.Scientific reports · 2026Article
- Mislocalization of KCNQ2 Channels as a Pathogenic Mechanism in KCNQ2 Developmental and Epileptic Encephalopathy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Article
- Pharmacological approaches in drug-resistant pediatric epilepsies caused by pathogenic variants in potassium channel genes.Frontiers in cellular neuroscience · 2024Article
- Corticotropin-releasing hormone neurons in the central nucleus of amygdala are required for chronic stress-induced hypertension.Cardiovascular research · 2023Article
- Polydisperse molecular architecture of connexin 26/30 heteromeric hemichannels revealed by atomic force microscopy imaging.The Journal of biological chemistry · 2020Article
- Familial neonatal seizures caused by the Kv7.3 selectivity filter mutation T313I.Epilepsia open · 2020Article
- Novel Analgesics with Peripheral Targets.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2020Review
- Determining the correct stoichiometry of Kv2.1/Kv6.4 heterotetramers, functional in multiple stoichiometrical configurations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Epileptic Encephalopathy In A Patient With A Novel Variant In The Kv7.2 S2 Transmembrane Segment: Clinical, Genetic, and Functional Features.International journal of molecular sciences · 2019Article
- Kv7.3 Compound Heterozygous Variants in Early Onset Encephalopathy Reveal Additive Contribution of C-Terminal Residues to PIPMolecular neurobiology · 2018Article
- PIP Water Transport and Its pH Dependence Are Regulated by Tetramer Stoichiometry.Biophysical journal · 2016Article
- Ability of naringenin, a bioflavonoid, to activate M-type potassium current in motor neuron-like cells and to increase BKCa-channel activity in HEK293T cells transfected with α-hSlo subunit.BMC neuroscience · 2014Article
- Heteromerization of PIP aquaporins affects their intrinsic permeability.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Genotype-phenotype correlations in neonatal epilepsies caused by mutations in the voltage sensor of K(v)7.2 potassium channel subunits.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Distinct subunit contributions to the activation of M-type potassium channels by PI(4,5)P2.The Journal of general physiology · 2012Article
- Surface expression and subunit specific control of steady protein levels by the Kv7.2 helix A-B linker.PloS one · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Voltage-gated K(+) channels composed of Kv7.2 and Kv7.3 are the predominant contributors to the M-current, which plays a key role in controlling neuronal activity. Various lines of evidence have indicated that Kv7.2 and Kv7.3 form a heteromeric channel. However, the subunit stoichiometry and arrangement within this putative heteromer are so far unknown. Here, we have addressed this question using atomic force microscopy imaging of complexes between isolated Kv7.2/Kv7.3 channels and antibodies to epitope tags on the two subunits, Myc on Kv7.2 and HA on Kv7.3. Initially, tsA 201 cells were transiently transfected with equal amounts of cDNA for the two subunits. The heteromer was isolated through binding of either tag to immunoaffinity beads and then decorated with antibodies to the other tag. In both cases, the distribution of angles between pairs of bound antibodies had two peaks, at around 90° and around 180°, and in both cases the 90° peak was about double the size of the 180° peak. These results indicate that the Kv7.2/Kv7.3 heteromer generated by cells expressing approximately equal amounts of the two subunits assembles as a tetramer with a predominantly 2:2 subunit stoichiometry and with a random subunit arrangement. When the DNA ratio for the two subunits was varied, copurification experiments indicated that the subunit stoichiometry was variable and not fixed at 2:2. Hence, there are no constraints on either the subunit stoichiometry or the subunit arrangement.
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