Ask about this productRelated genes to: KCNK4 antibody
- Gene:
- KCNK4 NIH gene
- Name:
- potassium two pore domain channel subfamily K member 4
- Previous symbol:
- -
- Synonyms:
- K2p4.1, TRAAK
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-04-13
- Date modifiied:
- 2016-10-05
Related products to: KCNK4 antibody
Related articles to: KCNK4 antibody
- KCNK4-associated gingival fibromatosis (K-GF) is a rare condition characterised by progressive gingival enlargement and excessive connective tissue accumulation. Although pathogenic variants in KCNK4 have been linked to syndromic gingival overgrowth, the cellular and molecular mechanisms underlying the gingival phenotype remain incompletely understood. This study aimed to investigate the biological effects of a rare heterozygous KCNK4 c.730G>C variant identified in a paediatric patient with K-GF and to explore its potential role in gingival fibroblast dysfunction. - Source: PubMed
Publication date: 2026/07/29
Wu YantongYang ShuranKong FanyingHe MingZhang YanZhang ShengnanZhou HongxianYang RuoxiMao YongjianShi HongZhang JieZhang Mingzhu - Epilepsy with febrile seizures plus (EFS+) is a syndrome with a strong genetic component. Previously, variants in several genes encoding ion channels have been associated with EFS+. However, the etiology in the majority of patients remains undetermined. - Source: PubMed
Publication date: 2025/03/31
Yan Hong-JunLiu Wen-HuiXu Min-XingWang Peng-YuGu Yu-JieLi HuaGuo JingLuo Sheng - Potassium ion channels play a crucial role in maintaining cellular electrical stability and are implicated in various epilepsies. Heterozygous pathogenic variants in KCNK4 cause a recognizable neurodevelopmental syndrome with facial dysmorphism, hypertrichosis, epilepsy, intellectual disability (ID), and gingival overgrowth (FHEIG). To date, no more than nine patients with FHEIG have been described worldwide and still little is known about epileptic phenotype in KCNK4-related disease. - Source: PubMed
Publication date: 2024/08/09
Krygier MagdalenaZiętkiewicz SzymonTalaśka-Liczbik WeronikaChylińska MagdalenaWalczak AnnaKostrzewa GrażynaPłoski RafałMazurkiewicz-Bełdzińska Maria - The axon initial segment (AIS) is a critical compartment in neurons. It converts postsynaptic input into action potentials that subsequently trigger information transfer to target neurons. This process relies on the presence of several voltage-gated sodium (Na) and potassium (K) channels that accumulate in high densities at the AIS. TRAAK is a mechanosensitive leak potassium channel that was recently localized to the nodes of Ranvier. Here, we uncover that TRAAK is also present in AISs of hippocampal and cortical neurons in the adult rat brain as well as in AISs of cultured rat hippocampal neurons. We show that the AIS localization is driven by a C-terminal ankyrin G-binding sequence that organizes TRAAK in a 190 nm spaced periodic pattern that codistributes with periodically organized ankyrin G. We furthermore uncover that while the identified ankyrin G-binding motif is analogous to known ankyrin G-binding motifs in Na1 and K7.2/K7.3 channels, it was acquired by convergent evolution. Our findings identify TRAAK as an AIS ion channel that convergently acquired an ankyrin G-binding motif and expand the role of ankyrin G to include the nanoscale organization of ion channels at the AIS. - Source: PubMed
Publication date: 2024/07/26
Luque-Fernández VirginiaVanspauwen Sam KLandra-Willm ArnaudArvedsen EmilBesquent MaïlysSandoz GuillaumeRasmussen Hanne B - TREK2, a two-pore domain potassium channel, is recognized for its regulation by various stimuli, including lipids. While previous members of the TREK subfamily, TREK1 and TRAAK, have been investigated to elucidate their lipid affinity and selectivity, TREK2 has not been similarly studied in this regard. Our findings indicate that while TRAAK and TREK2 exhibit similarities in terms of electrostatics and share an overall structural resemblance, there are notable distinctions in their interaction with lipids. Specifically, SAPI(4,5)P2,1-stearoyl-2-arachidonoyl--glycero-3-phospho-(1'-myo-inositol-4',5'-bisphosphate) exhibits a strong affinity for TREK2, surpassing that of dOPI(4,5)P2,1,2-dioleoyl--glycero-3-phospho-(1'-myo-inositol-4',5'-bisphosphate), which differs in its acyl chains. TREK2 displays lipid binding preferences not only for the headgroup of lipids but also toward the acyl chains. Functional studies draw a correlation for lipid binding affinity and activity of the channel. These findings provide important insight into elucidating the molecular prerequisites for specific lipid binding to TREK2 important for function. - Source: PubMed
Publication date: 2024/06/06
Stover LaurenZhu YunSchrecke SamanthaLaganowsky Arthur