Affinage

KCNJ15

ATP-sensitive inward rectifier potassium channel 15 · UniProt Q99712

Length
375 aa
Mass
42.6 kDa
Annotated
2026-06-10
30 papers in source corpus 20 papers cited in narrative 20 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

KCNJ15 encodes Kir4.2, an inwardly rectifying K+ channel whose biophysical identity and physiological roles are governed by its subunit composition and its position in the basolateral membrane of the renal proximal tubule (PMID:11306656, PMID:31870500). Homomeric Kir4.2 is a strong rectifier with ~25 pS conductance and high open probability, while association with Kir5.1 converts it into a weakly rectifying ~50–54 pS channel with bursting kinetics and sensitivity to intracellular acidification; Kir5.1 is also required for stable Kir4.2 protein expression and membrane assembly in the proximal tubule (PMID:11306656, PMID:16949552, PMID:39745541). Kir4.2 carries intrinsic intracellular pH sensitivity (pKa ~7.1) and, in its homomeric form, slowly senses extracellular K+ by altering transitions between channel states without changing surface density (PMID:11306656, PMID:22025665). In the proximal tubule Kir4.2 localizes exclusively to the basolateral membrane and sets membrane potential; its loss depolarizes the cell, alkalinizes the cytoplasm, raises the bicarbonate reabsorption threshold, and impairs ammoniagenesis, producing hyperchloremic metabolic acidosis (PMID:31870500). Functioning as a K+ sensor, Kir4.2 transduces dietary K+ deficiency into basolateral K+ flux, intracellular acidosis, and glutaminase-dependent ammoniagenesis that drives kidney injury and fibrosis, and it lies upstream of a Cl−/mTORC2/AKT axis controlling proximal tubule cell expansion (PMID:36543132, PMID:38886379); its baseline expression and activity are maintained by AT1a angiotensin receptor signaling (PMID:37909221). Beyond the kidney, Kir4.2 translocates from cytoplasmic vesicles to the apical membrane to supply K+ for histamine-stimulated gastric acid secretion (PMID:21719736, PMID:26108660), suppresses glucose-stimulated insulin secretion in pancreatic beta cells in part through physical interaction with the Ca2+-sensing receptor (PMID:17122384, PMID:22566534), and couples with intracellular polyamines to sense electric fields and direct galvanotaxis via PIP3 polarization (PMID:26449415). Surface expression is controlled by C-terminal trafficking determinants including a tyrosine phosphorylation site (PMID:17468958). A Parkinson's disease-linked R28C mutation causes dominant-negative loss of function through reduced protein stability, impaired glycosylation, and defective plasma membrane trafficking (PMID:40566643).

Mechanistic history

Synthesis pass · year-by-year structured walk · 20 steps
  1. 2001 High

    Established the fundamental biophysical identity of Kir4.2 and showed that heteromerization with Kir5.1 produces a distinct channel, defining the two functional forms of the channel.

    Evidence Single-channel and two-electrode voltage clamp in Xenopus oocytes with intracellular pH manipulation

    PMID:11306656

    Open questions at the time
    • pH-sensing C-terminal residues not mapped
    • native tissue subunit stoichiometry not addressed
  2. 2006 High

    Identified the Ca2+-sensing receptor as a direct C-terminal binding partner that suppresses Kir4.2 current, linking the channel to extracellular Ca2+ signaling.

    Evidence Yeast two-hybrid, reciprocal Co-IP in HEK293 and rat kidney, and oocyte electrophysiology with a non-functional CaR mutant control

    PMID:17122384

    Open questions at the time
    • mechanism by which CaR reduces current unresolved
    • physiological context of interaction not established in this study
  3. 2006 Medium

    Defined the rectification mechanism by which Kir5.1 converts Kir4.2 from a strong to a weak rectifier and confers pHi sensitivity.

    Evidence Whole-cell patch clamp and Mg2+ block kinetics in HEK293 cells using a Kir4.2-Kir5.1 fusion construct

    PMID:16949552

    Open questions at the time
    • fusion construct may not reflect native heterotetramer stoichiometry
    • single lab
  4. 2007 Medium

    Localized trafficking control to C-terminal determinants including a tyrosine phosphorylation site, explaining how surface expression is regulated post-translationally.

    Evidence Site-directed mutagenesis and two-electrode voltage clamp in Xenopus oocytes

    PMID:17468958

    Open questions at the time
    • kinase responsible not identified
    • phosphorylation not directly demonstrated
  5. 2010 Medium

    Showed a synonymous KCNJ15 SNP modulates mRNA stability and protein level, providing a genetic route to altered channel dosage.

    Evidence mRNA stability assay and protein quantification in HEK293 cells comparing risk and non-risk alleles

    PMID:20085713

    Open questions at the time
    • mechanism of mRNA stabilization unknown
    • in vivo physiological consequence not tested
  6. 2011 Medium

    Established Kir4.2 as a regulated K+ supply for gastric acid secretion via stimulus-dependent vesicle-to-apical-membrane translocation.

    Evidence Immunofluorescence and subcellular fractionation of isolated gastric glands

    PMID:21719736

    Open questions at the time
    • trafficking machinery not identified
    • functional necessity not yet tested at this stage
  7. 2011 Medium

    Placed Kir4.2 within an integrin/polyamine-driven glioma migration pathway, broadening its role beyond epithelial K+ handling.

    Evidence siRNA knockdown, barium and pharmacological channel block, and migration assays in glioma xenograft cells

    PMID:21946432

    Open questions at the time
    • direct biochemical link to SSAT/integrin not shown
    • channel activity vs. structural role not distinguished
  8. 2011 High

    Defined the mechanism of homomeric extracellular K+ sensing, showing it operates through channel-state transitions and is independent of pHi sensing and Kir5.1.

    Evidence Two-electrode voltage clamp, patch clamp, K66M mutagenesis, and kinetic modeling in oocytes

    PMID:22025665

    Open questions at the time
    • molecular K+-sensing site not identified
    • relevance to heteromeric channels excluded but native role unaddressed
  9. 2012 Medium

    Demonstrated Kir4.2 suppresses insulin secretion and re-confirmed the CaR interaction in a pancreatic context, extending the channel into glucose homeostasis.

    Evidence siRNA knockdown in INS1 cells and in mice with insulin secretion assays and Co-IP of Kir4.2 with CaR

    PMID:22566534

    Open questions at the time
    • electrical mechanism linking channel to secretion not resolved
    • single lab
  10. 2015 High

    Revealed Kir4.2 as a polyamine-coupled electric-field sensor required specifically for galvanotaxis through PIP3 polarization.

    Evidence RNAi screen, knockdown, polyamine manipulation, polyamine-binding mutant, and PIP3 imaging galvanotaxis assays

    PMID:26449415

    Open questions at the time
    • link from K+ flux to PIP3 redistribution mechanistically incomplete
    • in vivo relevance not established
  11. 2015 High

    Established that Kir4.2 is functionally required for histamine-stimulated gastric acid secretion, upgrading the earlier localization finding to causal necessity.

    Evidence shRNA knockdown in primary parietal cells with acid secretion assay and live-cell trafficking imaging

    PMID:26108660

    Open questions at the time
    • trafficking signal and machinery not defined
    • interaction with H+,K+-ATPase not biochemically mapped
  12. 2019 High

    Defined the renal physiological role of Kir4.2 as the basolateral K+ channel setting proximal tubule potential and enabling acid-base balance and ammoniagenesis.

    Evidence Kcnj15 knockout mice with patch clamp, intracellular pH, acid loading, and proximal tubule protein expression analysis

    PMID:31870500

    Open questions at the time
    • how depolarization links to ammonia metabolism protein changes not fully resolved
    • compensatory channels not characterized
  13. 2022 High

    Identified Kir4.2 as the K+-deficiency sensor driving glutaminase-dependent ammoniagenesis and kidney injury, with epistasis placing it upstream of glutaminase.

    Evidence Kir4.2 knockout mice in dietary K+ depletion and aldosteronism models with epistasis against glutaminase knockout

    PMID:36543132

    Open questions at the time
    • initial K+-sensing trigger at the molecular level not defined
    • human relevance not directly tested
  14. 2022 Medium

    Showed Kir4.2 supports RPE cell viability and is transcriptionally controlled by growth-factor receptor signaling, extending its role to ocular epithelium.

    Evidence siRNA knockdown, viability/proliferation assays, and receptor pharmacology (VEGFR2, TGF-β1, PDGF) in cultured RPE cells

    PMID:35740973

    Open questions at the time
    • channel-dependent vs. independent contribution to viability unclear
    • single lab
  15. 2023 Medium

    Connected angiotensin signaling to Kir4.2 by showing AT1aR maintains its baseline expression and mediates angiotensin II-induced proximal tubule hyperpolarization.

    Evidence Kidney-tubule-specific AT1aR knockout mice with Western blot and proximal tubule patch clamp

    PMID:37909221

    Open questions at the time
    • mechanism of AT1aR control over Kir4.2 expression unknown
    • direct vs. indirect regulation not distinguished
  16. 2023 Low

    Proposed a lysosomal role via KCNJ15–V-ATPase binding affecting drug accumulation and chemoresistance in breast cancer.

    Evidence Co-IP, lysosomal drug accumulation assay, and V-ATPase inhibitor treatment in breast cancer cells

    PMID:37274925

    Open questions at the time
    • single Co-IP without reciprocal validation reported in abstract
    • lysosomal localization of KCNJ15 not independently confirmed
    • mechanism of drug aggregation unresolved
  17. 2024 High

    Placed Kir4.2 upstream of a Cl−/mTORC2/AKT signaling axis driving proximal tubule cell expansion during K+ deficiency.

    Evidence Kir4.2 knockout mice with 3D tubule imaging, AKT phosphorylation, and isolated tubule mTORC2/Cl- manipulation

    PMID:38886379

    Open questions at the time
    • how Kir4.2 flux changes intracellular Cl- transport not detailed
    • direct mTORC2 activator not identified
  18. 2024 Medium

    Linked KCNJ15 to tumor suppression via GNB1 interaction and Hippo-YAP regulation in lung cancer.

    Evidence KCNJ15-GNB1 interaction assay, YAP phosphorylation Western blot, gain/loss-of-function in cell lines and xenografts

    PMID:39725264

    Open questions at the time
    • mechanism linking channel to YAP phosphorylation unclear
    • whether activity depends on K+ conductance not tested
  19. 2025 High

    Demonstrated that Kir5.1 is essential for assembling the native basolateral 50-pS heterotetramer and for stable Kir4.2 expression in the proximal tubule.

    Evidence Kir5.1 knockout mice with single-channel patch clamp, immunoblotting, and immunofluorescence

    PMID:39745541

    Open questions at the time
    • mechanism by which Kir5.1 stabilizes Kir4.2 unknown
    • fate of unassembled Kir4.2 not characterized
  20. 2025 High

    Established a disease mechanism for a Parkinson's-linked R28C mutation as dominant-negative loss of function via destabilization and trafficking defects.

    Evidence Patch clamp, Western blot, glycosylation analysis, and subcellular fractionation in HEK293T cells with WT/mutant co-expression

    PMID:40566643

    Open questions at the time
    • link between channel loss and neuronal pathology not established
    • in vivo neuronal phenotype not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • The molecular identity of the extracellular K+-sensing site and the precise coupling between Kir4.2 K+ flux and downstream signaling (Cl−/mTORC2/AKT, PIP3 polarization, YAP) remain undefined.
  • K+-sensor residues not mapped
  • structural basis of Kir5.1-dependent stabilization unknown
  • neuronal function relevant to Parkinson's disease uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005215 transporter activity 5 GO:0005198 structural molecule activity 2 GO:0140299 molecular sensor activity 2
Localization
GO:0005886 plasma membrane 5 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1430728 Metabolism 2 R-HSA-382551 Transport of small molecules 2
Partners
ATP6V (V-ATPASE)CASRGNB1KCNJ16
Complex memberships
Kir4.2/Kir5.1 heterotetramer

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 Kir4.2 (KCNJ15) forms heteromeric channels with Kir5.1. Homomeric Kir4.2 has high open probability (Po > 0.9) and ~25 pS conductance, while Kir4.2-Kir5.1 heteromers show bursting behavior (Po < 0.3) and ~54 pS conductance with subconductance states. Kir4.2 has higher intrinsic pH sensitivity (pKa = 7.1) than Kir4.1 (pKa = 5.99) due to an additional pH-sensing mechanism in the C-terminus; coexpression with Kir5.1 does not cause a major shift in pH sensitivity of the Kir4.2-Kir5.1 heteromer. Xenopus oocyte expression, cell-attached single-channel patch clamp, two-electrode voltage clamp, intracellular pH manipulation The Journal of physiology High 11306656
2006 The Ca2+-sensing receptor (CaR) physically interacts with Kir4.2 (KCNJ15) via the C-terminal ~125 aa of Kir4.2 (identified by yeast two-hybrid with the CaR C-terminal tail). Reciprocal co-immunoprecipitation confirmed the interaction in HEK-293 cells and in rat kidney extracts. Co-expression of CaR with Kir4.2 in Xenopus oocytes reduced whole-cell Kir4.2 currents; a non-functional CaR mutant (R796W) that fails to co-IP with Kir4.2 had no effect. Yeast two-hybrid, reciprocal co-immunoprecipitation (HEK-293 cells and rat kidney), two-electrode voltage clamp in Xenopus oocytes, loss-of-function CaR mutant American journal of physiology. Renal physiology High 17122384
2006 Association of Kir4.2 with Kir5.1 converts Kir4.2 from a strong to a weak rectifier: Kir4.2 homomers show rapid, voltage-independent Mg2+ block (strong rectifier), whereas Kir4.2-Kir5.1 heteromers have a significantly increased Mg2+ blocking time constant and increased steady-state outward current. Additionally, Kir5.1 renders Kir4.2 currents sensitive to mild intracellular acidification with pHi-dependent run-down. Whole-cell patch clamp and voltage-step protocols in HEK293 cells expressing Kir4.2 and Kir4.2-Kir5.1 fusion protein Biochimica et biophysica acta Medium 16949552
2007 The Kir4.2 C-terminus contains trafficking determinants that regulate plasma membrane expression. Truncation of the C-terminus increased current density in Xenopus oocytes. Mutation of a putative tyrosine phosphorylation site in a unique C-terminal region increased current density, suggesting tyrosine phosphorylation promotes channel retrieval from (or prevents trafficking to) the membrane. A previously identified residue K110N also increases current density by an independent mechanism (combining both mutations causes multiplicative increase). Xenopus oocyte expression, two-electrode voltage clamp, site-directed mutagenesis of C-terminal and internal regions The Journal of membrane biology Medium 17468958
2010 A synonymous SNP in exon 4 of KCNJ15 (rs3746876, C566T) increases KCNJ15 mRNA stability, resulting in higher protein expression in HEK293 cells carrying the risk allele compared to the non-risk allele. Functional analysis in HEK293 cells, mRNA stability assay, protein expression quantification American journal of human genetics Medium 20085713
2011 In resting gastric parietal cells, KCNJ15 is stored in small cytoplasmic vesicles distinct from H+,K+-ATPase-containing tubulovesicles. Upon stimulation, KCNJ15 translocates from these vesicles to the apical membrane where it co-localizes with H+,K+-ATPase, providing K+ for acid secretion. Immunofluorescence staining of isolated gastric glands, subcellular fractionation with sequential centrifugation (30-min 100,000g vs. 4-h 100,000g), Western blot of membrane fractions American journal of physiology. Gastrointestinal and liver physiology Medium 21719736
2011 The α9β1 integrin-mediated glioma cell migration pathway involves Kir4.2 downstream of SSAT (spermidine/spermine N1-acetyltransferase). Kir4.2 co-localizes with α9 integrin in glioma xenograft cells, and siRNA knockdown of Kir4.2 (or barium channel block) significantly inhibits cell migration driven by MMP-9/uPAR/cathepsin B overexpression. siRNA knockdown of Kir4.2 with migration assay, barium channel inhibition, co-localization by immunofluorescence, selective pharmacological inhibitors (glybenclamide, tertiapin-Q) Cellular signalling Medium 21946432
2011 Kir4.2 homomeric channel activity is regulated by extracellular K+ concentration ([K+]o) in a slow (tens of minutes) manner. This regulation is specific to the homomeric form and is abolished by co-expression with Kir5.1. K+o-dependent activation does not involve increased surface expression of the channel, nor differences in open probability; instead, K+o affects the rate of transition between channel states at the plasma membrane. The K+o sensitivity is independent of intracellular pH sensitivity (K66M mutation abolishes pHi sensitivity without affecting K+o sensitivity). Two-electrode voltage clamp in Xenopus oocytes, patch clamp, site-directed mutagenesis (K66M), kinetic modeling The Journal of physiology High 22025665
2012 Kcnj15 knockdown in INS1 cells and in vivo in mice increases glucose-stimulated insulin secretion, demonstrating that Kir4.2 suppresses insulin secretion. Additionally, Kir4.2 interacts with the Ca2+-sensing receptor (CsR) in INS1 pancreatic beta cells (as it does in kidney), and this interaction is part of the mechanism regulating insulin secretion. siRNA knockdown in INS1 cells (in vitro), siRNA injection in normal and diabetic mice (in vivo), insulin secretion assay, co-immunoprecipitation of Kir4.2 with CsR in INS1 cells Diabetes Medium 22566534
2015 KCNJ15/Kir4.2 knockdown specifically abolishes galvanotaxis (directed cell migration in an electric field) without affecting basal motility or monolayer scratch migration. Intracellular polyamines couple with Kir4.2 to mediate electric field sensing: polyamine depletion abolishes galvanotaxis in a Kir4.2-dependent manner, polyamine increase enhances it, and a polyamine-binding defective KCNJ15 mutant reduces galvanotaxis. Furthermore, Kir4.2 knockdown prevents PIP3 redistribution to the leading edge in response to the electric field. RNAi library screen, siRNA knockdown, galvanotaxis assay, polyamine depletion/supplementation, polyamine-binding mutant expression, PIP3 redistribution imaging Nature communications High 26449415
2015 KCNJ15 is required for histamine-stimulated gastric acid secretion. shRNA-mediated knockdown of KCNJ15 in rabbit primary parietal cells abolishes histamine-stimulated acid secretion. Live cell imaging confirmed that KCNJ15 translocates from cytoplasmic puncta to the apical membrane upon stimulation. shRNA adenoviral knockdown in primary parietal cells, acid secretion assay, live cell imaging of KCNJ15 trafficking American journal of physiology. Cell physiology High 26108660
2019 Kir4.2 (Kcnj15 gene product) is localized exclusively at the basolateral membrane of proximal tubular cells. Kcnj15 knockout in mice causes hyperchloremic metabolic acidosis with reduced bicarbonate reabsorption threshold, impaired ammonium excretion (inappropriate for the degree of acidosis), and decreased expression of proximal ammonia metabolism proteins (glutamine transporter SNAT3, phosphate-dependent glutaminase, PEPCK, NHE-3). Kcnj15 deletion depolarizes the proximal cell membrane by reducing barium-sensitive K+ conductance and causes intracellular alkalinization. Kcnj15 knockout mouse model, immunofluorescence (exclusive basolateral localization), acid-base balance measurements, metabolic acid loading, patch clamp (basolateral K+ conductance), intracellular pH measurement, Western blot of proximal tubule proteins Kidney international High 31870500
2022 Kir4.2 mediates direct kidney injury caused by dietary K+ deficiency. In response to reduced blood K+, Kir4.2 mediates altered proximal tubule basolateral K+ flux causing intracellular acidosis and activation of glutaminase and the ammoniagenesis pathway. Deletion of either Kir4.2 or glutaminase protects from low-K+ induced kidney injury and fibrosis. Kir4.2 knockout mice, dietary K+ depletion model, aldosteronism model, urinary K+ excretion, kidney injury/fibrosis assessment, epistasis with glutaminase knockout Cell reports High 36543132
2023 AT1aR (angiotensin II type 1a receptor) controls baseline expression and activity of Kir4.2 in proximal tubule. Kidney-tubule-specific AT1aR knockout mice show reduced Kir4.2 expression and a less-negative proximal tubule membrane potential, while AT1aR is required for angiotensin II-induced hyperpolarization of the proximal tubule basolateral membrane. Kidney-tubule-specific AT1aR knockout mice, Western blot for Kir4.2 expression, whole-cell patch clamp of proximal tubule membrane potential, angiotensin II infusion Hypertension Medium 37909221
2023 KCNJ15 protein binds to V-ATPase at the lysosome surface. KCNJ15 deficiency in breast cancer cells leads to drug aggregation in lysosomes (altered lysosomal function) and reduces drug efficacy. A V-ATPase inhibitor disrupts the KCNJ15–V-ATPase interaction, contributing to drug resistance reversal. Co-immunoprecipitation/protein-protein interaction assay (KCNJ15 and V-ATPase), lysosomal drug accumulation assay, V-ATPase inhibitor treatment, KCNJ15 knockdown in breast cancer cells Asian journal of pharmaceutical sciences Low 37274925
2024 Low dietary K+ activates AKT/mTORC2 signaling in proximal tubule in a Kir4.2-dependent manner. Kir4.2 knockout mice fail to undergo proximal tubule cell expansion in response to K+ deficiency and show blunted AKT phosphorylation. In isolated tubules, AKT phosphorylation in response to low K+ depends on mTORC2 activation by secondary changes in intracellular Cl- transport, placing Kir4.2 upstream of a Cl-/mTORC2/AKT signaling axis. Kir4.2 knockout mice, dietary K+ depletion, 3D imaging of proximal tubule volume, AKT phosphorylation (Western blot), isolated tubule experiments with Cl- transport manipulation, mTORC2 inhibition Nature communications High 38886379
2025 Kir5.1 is essential for assembling the basolateral 50-pS inwardly rectifying K+ channel (Kir4.2/Kir5.1 heterotetramer) in mouse proximal tubule. Kir5.1 knockout abolishes the 50-pS channel in the proximal tubule basolateral membrane, reduces Kir4.2 protein expression and membrane localization, and depolarizes the proximal tubule membrane potential. Kir5.1 knockout mice, single-channel patch clamp of proximal tubule basolateral membrane, immunoblotting, immunofluorescence staining American journal of physiology. Renal physiology High 39745541
2025 The Parkinson's disease-linked KCNJ15 mutation R28C causes loss of Kir4.2 channel function with dominant-negative effects. The mutant protein shows reduced overall expression, reduced stability, impaired glycosylation efficiency, and compromised plasma membrane trafficking compared to wild-type Kir4.2. Both wild-type and R28C undergo post-translational glycosylation with differing protein turnover efficiencies. Patch clamp electrophysiology in Kir4.2-overexpressing HEK293T cells, Western blot (protein expression and glycosylation), subcellular fractionation (plasma membrane trafficking), dominant-negative assay (co-expression of WT and mutant) The Journal of physiology High 40566643
2024 KCNJ15 interacts with GNB1 (G protein subunit beta 1) and regulates the Hippo-YAP pathway. KCNJ15 overexpression activates YAP phosphorylation and inhibits YAP expression; GNB1 overexpression reduces these KCNJ15-mediated effects on the Hippo pathway. KCNJ15 overexpression inhibits lung cancer cell growth, invasion, and migration in vitro and in vivo. Protein-protein interaction assay (KCNJ15-GNB1), YAP phosphorylation Western blot, KCNJ15 overexpression and knockdown in cell lines, xenograft tumor model Toxicology Medium 39725264
2022 Kir4.2 channels contribute to viability and proliferation of retinal pigment epithelial (RPE) cells. siRNA-mediated knockdown of Kir4.2 decreases RPE cell viability and proliferation under both normal and hyperosmotic conditions. VEGF downregulates Kir4.2 expression via VEGF receptor-2 activation; hyperosmotic Kir4.2 upregulation is mediated by TGF-β1 receptor signaling, while hypoxic upregulation depends on PDGF receptor signaling. siRNA knockdown in cultured RPE cells, cell viability/proliferation assays, VEGF receptor-2 blockade, qRT-PCR, Western blot Biomolecules Medium 35740973

Source papers

Stage 0 corpus · 30 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Differential pH sensitivity of Kir4.1 and Kir4.2 potassium channels and their modulation by heteropolymerisation with Kir5.1. The Journal of physiology 120 11306656
2015 KCNJ15/Kir4.2 couples with polyamines to sense weak extracellular electric fields in galvanotaxis. Nature communications 98 26449415
2006 Interaction of the Ca2+-sensing receptor with the inwardly rectifying potassium channels Kir4.1 and Kir4.2 results in inhibition of channel function. American journal of physiology. Renal physiology 74 17122384
2010 Identification of KCNJ15 as a susceptibility gene in Asian patients with type 2 diabetes mellitus. American journal of human genetics 49 20085713
1997 A new inward rectifier potassium channel gene (KCNJ15) localized on chromosome 21 in the Down syndrome chromosome region 1 (DCR1). Genomics 47 9299242
2012 Inhibition of glucose-stimulated insulin secretion by KCNJ15, a newly identified susceptibility gene for type 2 diabetes. Diabetes 41 22566534
2019 Defective bicarbonate reabsorption in Kir4.2 potassium channel deficient mice impairs acid-base balance and ammonia excretion. Kidney international 33 31870500
2011 Integrin α9β1-mediated cell migration in glioblastoma via SSAT and Kir4.2 potassium channel pathway. Cellular signalling 33 21946432
2011 Acid secretion-associated translocation of KCNJ15 in gastric parietal cells. American journal of physiology. Gastrointestinal and liver physiology 26 21719736
2022 Kir4.2 mediates proximal potassium effects on glutaminase activity and kidney injury. Cell reports 21 36543132
2000 Developmentally regulated expression of the murine ortholog of the potassium channel KIR4.2 (KCNJ15). Mechanisms of development 19 10906485
2020 KCNJ15 Expression and Malignant Behavior of Esophageal Squamous Cell Carcinoma. Annals of surgical oncology 17 32052303
2015 Potassium channel KCNJ15 is required for histamine-stimulated gastric acid secretion. American journal of physiology. Cell physiology 17 26108660
2023 KCNJ15 deficiency promotes drug resistance via affecting the function of lysosomes. Asian journal of pharmaceutical sciences 9 37274925
2006 Modulation of Kir4.2 rectification properties and pHi-sensitive run-down by association with Kir5.1. Biochimica et biophysica acta 9 16949552
2024 Low potassium activation of proximal mTOR/AKT signaling is mediated by Kir4.2. Nature communications 8 38886379
2011 Potassium-dependent activation of Kir4.2 K⁺ channels. The Journal of physiology 8 22025665
2013 Replication study for the association of a single-nucleotide polymorphism, rs3746876, within KCNJ15, with susceptibility to type 2 diabetes in a Japanese population. Journal of human genetics 7 23595124
2023 Role of Angiotensin II Type 1a Receptor (AT1aR) of Renal Tubules in Regulating Inwardly Rectifying Potassium Channels 4.2 (Kir4.2), Kir4.1, and Epithelial Na+ Channel (ENaC). Hypertension (Dallas, Tex. : 1979) 6 37909221
2022 Integrative Analyses Identify KCNJ15 as a Candidate Gene in Patients with Epilepsy. Neurology and therapy 5 36168094
2007 C-terminal determinants of Kir4.2 channel expression. The Journal of membrane biology 5 17468958
2023 Exploring the common diagnostic gene KCNJ15 and shared pathway of ankylosing spondylitis and ulcerative colitis through integrated bioinformatics. Frontiers in physiology 4 37215183
2024 The Identification of Goat KCNJ15 Gene Copy Number Variation and Its Association with Growth Traits. Genes 3 38397239
2024 Advancing Kir4.2 Channel Ligand Identification through Collision-Induced Affinity Selection Mass Spectrometry. ACS chemical biology 3 38449446
2016 Association of the Single Nucleotide Polymorphisms in RUNX1, DYRK1A, and KCNJ15 with Blood Related Traits in Pigs. Asian-Australasian journal of animal sciences 3 27492348
2025 Kir5.1 regulates Kir4.2 expression and is a key component of the 50-pS inwardly rectifying potassium channel in basolateral membrane of mouse proximal tubules. American journal of physiology. Renal physiology 2 39745541
2025 The physiological characteristics of inward rectifying potassium channel Kir4.2 and its research progress in human diseases. Frontiers in cell and developmental biology 2 40342929
2025 Parkinson's disease-linked Kir4.2 mutation R28C leads to loss of ion channel function. The Journal of physiology 2 40566643
2022 Kir4.2 Potassium Channels in Retinal Pigment Epithelial Cells In Vitro: Contribution to Cell Viability and Proliferation, and Down-Regulation by Vascular Endothelial Growth Factor. Biomolecules 2 35740973
2024 KCNJ15 inhibits chemical-induced lung carcinogenesis and progression through GNB1 mediated Hippo pathway. Toxicology 0 39725264

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