KCNK10 antibody - C-terminal region (ARP35325_T100)
- Known as:
- KCNK10 (anti-) - C-terminal region (ARP35325_T100)
- Catalog number:
- arp35325_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- KCNK10 antibody - C-terminal region (ARP35325_T100)
Related genes to: KCNK10 antibody - C-terminal region (ARP35325_T100)
- Gene:
- KCNK10 NIH gene
- Name:
- potassium two pore domain channel subfamily K member 10
- Previous symbol:
- -
- Synonyms:
- K2p10.1, TREK-2, TREK2, PPP1R97
- Chromosome:
- 14q31.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-11
Related products to: KCNK10 antibody - C-terminal region (ARP35325_T100)
Related articles to: KCNK10 antibody - C-terminal region (ARP35325_T100)
- Langya chickens, a Chinese indigenous breed, exhibit rich genetic resources but relatively low egg production performance. To investigate the genetic basis of egg production traits, we performed low-depth genome resequencing of 1,183 Langya hens and evaluated six phenotypic traits, including age at first egg (AFE), egg number at different laying stages-EN1 (from first egg to 26 weeks), EN2 (27-36 weeks), EN3 (37-43 weeks), total egg number at 43 weeks (E43), and maximal clutch length (MCL). Genetic parameter analysis revealed that MCL exhibited high heritability (0.42) and strong genetic correlations with both egg production and AFE, suggesting its potential as a more effective selection indicator for egg production traits. Genome-wide association studies identified a total of 245 SNPs associated with these traits. Notably, a 6.58 Mb region on chromosome 5 (GGA5, 40.03-46.61 Mb) was enriched for multiple traits and in strong linkage disequilibrium. Candidate genes in this core region, including TSHR, GTF2A1, DIO2, STON2, NRXN3, KCNK10, EML5, and FOXN3, were implicated in transcriptional regulation, thyroid hormone signaling, neuroendocrine modulation, and ovarian function. Additional trait-specific candidate genes, such as ATG2B for EN2, FMNL1 for EN1/EN2, TDP1 for E43, and TPMT for MCL, were also identified. Functional enrichment analyses highlighted pathways related to cellular processes, lipid metabolism, and signal transduction. These findings provide genomic insights into the molecular mechanisms underlying egg production traits and offer valuable candidate genes for marker-assisted breeding in Langya chickens. - Source: PubMed
Publication date: 2026/01/04
Zhang HongruiFu YuanjieWang YanlinYin SijingJiang YunliangSun YiKang Li - TREK-1 (K2.1) and TREK-2 (K10.1) background K channels are widely expressed determinants of cellular excitability. We examined the regulation of TREK channels by the increase of cytoplasmic calcium concentration in Xenopus oocytes. Extracellular application of ionomycin, as well as the microinjection of inositol 1,4,5-trisphosphate (IP), evoked TREK-1 activation, whereas the microinjection of EGTA prevented the effect. TRAAK (K4.1) was not affected, whereas TREK-2 was activated by ionomycin in the presence of ML-335 K activator compound. Cyclosporin A and FK506, specific inhibitors of the calcium/calmodulin-dependent protein phosphatase (calcineurin), abrogated the activation of TREK channels by ionomycin. Coexpression of a constitutively active form of calcineurin with TREK-1 increased the background K current, but FK506 restored the basal channel activity. Mutations of TREK-1 phosphorylation sites (S300A/S333A) eliminated the response to ionomycin. Coexpression of the known interaction partner AKAP5 (AKAP79/AKAP150) with TREK-1 significantly enhanced the calcium-dependent activation. The wild-type anchoring protein induced higher TREK activation than a dominant negative AKAP5 construct carrying mutations in the PXIXIT-like calcineurin binding site. In conclusion, TREK-1 and TREK-2 are regulated in a calcium-dependent manner, in addition to the previously described TRESK (K18.1), however, TREK channels are activated by calcineurin anchored to AKAP5. - Source: PubMed
Publication date: 2025/12/29
Baukál DóraPergel EnikőDebreczeni DorinaHorváth ÁrminTóth Dániel JTakács Panna TCzirják Gábor - TWIK-related K channel (TREK)-2, expressed in sensory neurons, is involved in setting membrane potential, and its modulations contributes to the generation of nociceptive signals. Although acute and chronic pain is a common symptom experienced by patients with various conditions, most existing analgesics exhibit low efficacy and are associated with adverse effects. For this reason, finding the novel modulator of TREK-2 is of significance for the development of new analgesics. Recent studies have shown that α-Mangostin (α-MG) activates TREK-2, facilitating analgesic effects, yet the underlying molecular mechanisms remain elusive. Intriguingly, even though norfluoxetine (NFx) is known to inhibit TREK-2, α-MG is also observed to share a same binding site with NFx, and this implies that TREK-2 might be modulated in a highly complicated manner. Therefore, we examine the mechanism of how TREK-2 is activated by α-MG using computational methods and patch clamp experiments in the present study. Based on these results, we offer an explanation of how α-MG and NFx exhibit opposing effects at the same binding site of TREK-2. These findings will broaden our understanding of TREK-2 modulation, providing clues for designing novel analgesic drugs. - Source: PubMed
Publication date: 2024/10/21
Kim GangraeVan Nhung Thi HongNam Joo HyunLee Wook - 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 - The two-pore domain potassium (K) channels TREK-1 and TREK-2 link neuronal excitability to a variety of stimuli including mechanical force, lipids, temperature and phosphorylation. This regulation involves the C-terminus as a polymodal stimulus sensor and the selectivity filter (SF) as channel gate. Using crystallographic up- and down-state structures of TREK-2 as a template for full atomistic molecular dynamics (MD) simulations, we reveal that the SF in down-state undergoes inactivation via conformational changes, while the up-state structure maintains a stable and conductive SF. This suggests an atomistic mechanism for the low channel activity previously assigned to the down state, but not evident from the crystal structure. Furthermore, experimentally by using (de-)phosphorylation mimics and chemically attaching lipid tethers to the proximal C-terminus (pCt), we confirm the hypothesis that moving the pCt towards the membrane induces the up-state. Based on MD simulations, we propose two gating pathways by which movement of the pCt controls the stability (i.e., conductivity) of the filter gate. Together, these findings provide atomistic insights into the SF gating mechanism and the physiological regulation of TREK channels by phosphorylation. - Source: PubMed
Publication date: 2024/05/31
Türkaydin BerkeSchewe MarcusRiel Elena BarbaraSchulz FriederikeBiedermann JohannBaukrowitz ThomasSun Han