Affinage

KCNJ1

ATP-sensitive inward rectifier potassium channel 1 · UniProt P48048

Length
391 aa
Mass
44.8 kDa
Annotated
2026-04-28
96 papers in source corpus 41 papers cited in narrative 40 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

KCNJ1 (Kir1.1/ROMK) is an inwardly rectifying potassium channel that mediates K⁺ secretion in the distal nephron and K⁺ recycling for H⁺/K⁺-ATPase function in gastric parietal cells (PMID:26728465, PMID:25127675). Channel open probability is controlled by intracellular pH through a steric gate formed by Leu160 at the inner helix bundle crossing, with multiple C-terminal histidines serving as pH sensors, while PIP₂ binding at a proximal C-terminal arginine-rich domain is obligatory for channel opening and is enhanced by PKA phosphorylation via AKAP scaffolding (PMID:15653740, PMID:10713095, PMID:12381730, PMID:10318968, PMID:9707637). Surface expression is dynamically regulated: PKC phosphorylation at S4/S201 is required for plasma membrane delivery, c-Src phosphorylation at Y337 drives dynamin-dependent endocytosis, monoubiquitination at K22 by the E3 ligase POSH promotes internalization, and WNK kinases (WNK1/3/4) reduce surface abundance through intersectin-dependent clathrin-mediated endocytosis independently of their kinase activity (PMID:12221079, PMID:11719519, PMID:19710010, PMID:17380208). Loss-of-function mutations in the gene cause antenatal Bartter syndrome, with disease-relevant mutations in the intracellular immunoglobulin-like domain impairing channel folding, trafficking, and gating (PMID:10532965, PMID:19221509).

Mechanistic history

Synthesis pass · year-by-year structured walk · 20 steps
  1. 1994 High

    Cloning of KCNJ1 revealed it encodes a Ba²⁺-sensitive inwardly rectifying K⁺ channel with multiple alternatively spliced isoforms from a single locus, establishing the molecular identity of the renal secretory K⁺ channel.

    Evidence cDNA cloning, chromosomal mapping by FISH, functional expression in Xenopus oocytes

    PMID:8190102

    Open questions at the time
    • Nephron segment-specific functions of individual splice variants were unknown
    • Regulatory mechanisms governing channel activity had not been explored
  2. 1994 High

    Demonstrating that PKA phosphorylation restores channel activity after rundown established that ROMK is tonically regulated by a phosphorylation–dephosphorylation cycle, raising the question of how PKA is coupled to the channel.

    Evidence Excised inside-out patch clamp with exogenous PKA catalytic subunit and phosphatase inhibitors

    PMID:8058760

    Open questions at the time
    • Identity of the PKA anchoring mechanism was unknown
    • Whether PKA acts directly on the channel or through an intermediary was unresolved
  3. 1996 High

    Chimeric channel studies between ROMK1 and pH-insensitive IRK1 showed that extracellular K⁺ sensing maps to the core pore region while pH gating maps to the N-terminus, establishing that these two regulatory modalities are structurally separable.

    Evidence N-terminal chimera construction with two-electrode voltage clamp in oocytes

    PMID:8663367

    Open questions at the time
    • The molecular identity of pH-sensing residues was not determined
    • Location of the physical gate was unknown
  4. 1998 High

    Discovery that AKAP79 is required for cAMP/PKA responsiveness of ROMK1 resolved how PKA is functionally coupled to the channel — through a scaffolding protein that localizes PKA to the channel.

    Evidence Co-expression of AKAP79 with ROMK1 in oocytes; RII overlay on kidney membranes

    PMID:9707637

    Open questions at the time
    • Whether AKAP directly binds ROMK1 or acts through an intermediary was unresolved
    • The PKA phosphorylation sites on ROMK had not been linked to a downstream effector mechanism
  5. 1998 High

    State-dependent thiol modification of cysteines at positions 49 (N-terminus) and 308 (C-terminus) showed that pH gating involves coordinated conformational changes in both cytoplasmic domains, advancing understanding beyond the N-terminal chimera mapping.

    Evidence Systematic cysteine mutagenesis with state-dependent sulfhydryl reagent modification and patch clamp

    PMID:9852128

    Open questions at the time
    • The transmembrane location of the physical gate remained unknown
    • Identity of pH-sensing residues was still unresolved
  6. 1999 High

    Linking PKA phosphorylation to enhanced PIP₂ interaction established the mechanistic basis for PKA activation: PKA does not directly open the channel but lowers the PIP₂ threshold for channel activation, unifying phosphorylation and lipid regulation.

    Evidence Inside-out patch clamp with anti-PIP₂ antibodies, ATP[γS] as PKA substrate, PKA site mutagenesis

    PMID:10318968

    Open questions at the time
    • The PIP₂ binding site on the channel had not been mapped
    • How PKC and other kinases intersect with PIP₂ regulation was unknown
  7. 2000 High

    Identification of Y337 as the c-Src phosphorylation site controlling ROMK1 endocytosis versus exocytosis established tyrosine phosphorylation as a bidirectional trafficking switch, with multiple C-terminal histidines (H225, H274, H342, H354) concurrently identified as pH/CO₂ sensors.

    Evidence c-Src co-expression, PTK/PTP pharmacology, Y337A mutagenesis, microtubule disruption (oocytes and HEK293); systematic histidine mutagenesis with CO₂ sensitivity measurements

    PMID:10713095 PMID:11114300

    Open questions at the time
    • The endocytic machinery involved (dynamin, clathrin) had not been characterized
    • How dietary K⁺ signals converge on the Y337 pathway in vivo was unknown
  8. 2001 High

    Showing that Y337 tyrosine phosphorylation triggers dynamin-dependent endocytosis while dephosphorylation drives SNARE-dependent exocytosis completed the trafficking model, with the SUR2B interaction domain mapped to the ROMK1 N-terminal 'IRA' motif.

    Evidence Dominant-negative dynamin K44A, tetanus toxin inhibition of exocytosis, GFP-ROMK1 imaging, biotin labeling; N-terminal deletion/substitution mutagenesis and co-IP for SUR2B interaction

    PMID:11567030 PMID:11719519 PMID:12556363

    Open questions at the time
    • The E3 ubiquitin ligase involved in ROMK internalization was unknown
    • Whether clathrin-dependent or -independent pathways mediate endocytosis was not resolved
  9. 2002 High

    Three advances converged: PKC phosphorylation sites S4/S201 were shown essential for surface expression; SGK1/NHERF2 were identified as cooperative stimulators of channel trafficking; and the PIP₂/ATP binding site was mapped to a 39-amino-acid C-terminal region with critical arginines R188/R203/R217.

    Evidence In vitro ³²P phosphorylation, S4/S201 mutagenesis, confocal and biotin labeling (PKC); oocyte co-expression with brefeldin A (SGK1/NHERF2); MBP fusion binding assay with TNP-ATP and PIP₂ competition (binding site)

    PMID:12221079 PMID:12381730 PMID:12444200

    Open questions at the time
    • How SGK1 phosphorylation of ROMK alters pH sensitivity was not yet shown
    • Physiological stimuli upstream of PKC and SGK1 at the channel were not defined
  10. 2003 Medium

    SGK1 was shown to phosphorylate ROMK1 at Ser44, shifting pH sensitivity to more acidic values, through a mechanism requiring the NHERF2 PDZ scaffold — linking kinase, scaffold, and gating modulation into a single regulatory axis.

    Evidence Pull-down assays, S44 mutagenesis, oocyte voltage clamp, chemiluminescence surface expression

    PMID:12878206 PMID:14623317

    Open questions at the time
    • Whether SGK1-NHERF2-ROMK complex forms in native kidney was not demonstrated
    • The interplay between SGK1 and WNK pathways on ROMK was unknown
  11. 2005 High

    The pH gate was physically localized to Leu160 at the inner helix bundle crossing (steric gate requiring both size and hydrophobicity), and monoubiquitination at K22 was identified as a signal reducing surface expression in native kidney, establishing two fundamentally distinct regulatory mechanisms.

    Evidence L160 mutagenesis with homology modeling and patch clamp (gate); immunoprecipitation from renal cortex with systematic lysine mutagenesis and biotin labeling (ubiquitination)

    PMID:15653740 PMID:15767585

    Open questions at the time
    • The E3 ligase responsible for K22 ubiquitination was unidentified
    • How pH-sensor histidines communicate to the L160 gate was structurally unresolved
  12. 2006 High

    Cysteine accessibility experiments pinpointed position 175 in M2 as the site of pH-dependent pore occlusion, and CFTR was shown to be required for ATP sensitivity of native ROMK channels in TAL, revealing an unexpected functional coupling between two channels.

    Evidence State-dependent MTS modification at engineered cysteine 175 in macropatches (gate); patch clamp in native TAL cells from CFTR knockout and ΔF508 mice (CFTR coupling)

    PMID:16470247 PMID:16891366

    Open questions at the time
    • The molecular mechanism of CFTR-ROMK coupling was not elucidated
    • How the L160 steric gate and position 175 conformational change relate structurally was unclear
  13. 2007 High

    WNK1 and WNK4 were shown to stimulate ROMK1 endocytosis through a kinase-activity-independent mechanism involving proline-rich motif interactions with the endocytic scaffold intersectin, with disease-causing WNK4 mutations enhancing this interaction — directly linking pseudohypoaldosteronism type II genetics to ROMK trafficking.

    Evidence Co-IP, surface expression and endocytosis assays in heterologous cells, proline-rich motif mutagenesis

    PMID:17380208

    Open questions at the time
    • Whether WNK-intersectin-mediated endocytosis is clathrin-dependent in native tubules was unconfirmed
    • Downstream kinases (SPAK/OSR1) in this pathway had not been tested on ROMK
  14. 2009 High

    Multiple structural and regulatory insights converged: POSH was identified as the E3 ligase for ROMK1 ubiquitination driving dynamin-dependent endocytosis; FRET measurements showed N/C-terminal separation during pH-dependent opening; Bartter mutations in the IgLD impaired folding/trafficking; and an intersubunit salt bridge (R128-E132) was shown to prevent C-type-like inactivation.

    Evidence In vitro ubiquitination assay and RING domain deletion (POSH); FRET with ECFP/EYFP fusions (conformation); computational thermodynamic stability with trafficking assay (IgLD); mutagenesis with Ba²⁺/tertiapin-Q rescue (salt bridge)

    PMID:19221509 PMID:19272129 PMID:19686653 PMID:19710010

    Open questions at the time
    • Whether POSH-mediated ubiquitination is regulated by dietary K⁺ in vivo was unknown
    • Complete structural model of the cytoplasmic domain during gating transitions was lacking
  15. 2010 Medium

    Angiotensin II was shown to inhibit ROMK through a dual mechanism — PKC-activated c-Src phosphorylation at Y337 and enhancement of WNK4-mediated inhibition — integrating hormonal signaling with the previously characterized kinase and trafficking pathways.

    Evidence Perforated patch clamp in HEK293 cells, Western blot for pY337, losartan/PKC/PTK inhibitors, Y337A mutagenesis, native CCD patch clamp

    PMID:20927043

    Open questions at the time
    • Whether aldosterone opposes Ang II effects on ROMK through SGK1 in the same cells was not tested
    • In vivo confirmation with Ang II receptor knockout was lacking
  16. 2011 High

    Knockout-validated immunolocalization showed that high-K⁺ diet dramatically increases apical ROMK expression selectively in DCT2/CNT/CD (not DCT1), with increased mature glycosylation — establishing the in vivo nephron-segment specificity of K⁺-adaptive ROMK trafficking.

    Evidence ROMK-specific antibodies validated on Romk⁻/⁻ mice, segmental markers, glycosylation analysis, dietary K⁺ manipulation

    PMID:21454252

    Open questions at the time
    • The signaling pathway linking plasma K⁺ to increased ROMK glycosylation/trafficking was unidentified
    • Whether WNK-SPAK axis mediates the segment-specific response was not tested
  17. 2014 High

    SPAK/OSR1 were shown to reduce ROMK1 surface expression in a kinase-activity-dependent manner, and Kir1.1 knockout revealed an essential role in gastric acid secretion by providing K⁺ recycling for H⁺/K⁺-ATPase — extending ROMK function beyond the kidney.

    Evidence Constitutively active and kinase-dead SPAK/OSR1 mutants with oocyte voltage clamp (SPAK/OSR1); Kir1.1⁻/⁻ mice with whole-stomach and perfused gland acid secretion, tertiapin-Q inhibition (gastric)

    PMID:25127675 PMID:25322850

    Open questions at the time
    • Whether WNK kinases activate SPAK/OSR1 to reduce ROMK in the same signaling cascade was not directly demonstrated
    • Compensatory K⁺ channels in ROMK⁻/⁻ stomach were not characterized
  18. 2015 High

    c-Src was shown to phosphorylate WNK4 at Y1092/Y1094 (required for WNK4-mediated ROMK inhibition) and Y1143 (required for PTP-1D binding and SGK1 reversal), establishing WNK4 itself as a regulated signaling node integrating c-Src and SGK1 inputs onto ROMK.

    Evidence Mass spectrometry phosphosite identification, Co-IP with PTP-1D, WNK4 tyrosine mutagenesis, functional ROMK assay

    PMID:25805816

    Open questions at the time
    • In vivo confirmation that these WNK4 tyrosine phosphorylation events regulate ROMK in native kidney was not provided
    • Whether other WNK isoforms are similarly tyrosine-phosphorylated was not explored
  19. 2016 High

    Isoform-specific ROMK1 knockout demonstrated that ROMK1 is dispensable for NKCC2 activity in TAL but required for dietary K⁺-induced K⁺ secretion in the collecting duct, resolving the specific physiological role of the ROMK1 splice variant.

    Evidence Cre-LoxP deletion of Romk1-specific exon 1, patch clamp of CCD SK channels, dietary K⁺ challenge

    PMID:26728465

    Open questions at the time
    • Which ROMK isoform mediates K⁺ recycling in the TAL remains to be determined with isoform-specific knockouts
    • Compensatory upregulation of BK or other K⁺ channels in Romk1⁻/⁻ CCD was not fully characterized
  20. 2017 Medium

    NHERF1 was shown to be required for ROMK1 surface expression in collecting duct cells, and Asn171 was identified as the critical pore-lining residue for VU590 inhibitor block, advancing both the physiological scaffold requirements and pharmacological targeting of the channel.

    Evidence NHERF1 siRNA knockdown in M-1 cells with biotinylation and patch clamp; N171 mutagenesis with molecular modeling and electrophysiology

    PMID:28533091 PMID:28619748

    Open questions at the time
    • Whether NHERF1 and NHERF2 serve redundant or distinct roles at the apical membrane is unresolved
    • No high-resolution structure of ROMK with VU590 bound exists

Open questions

Synthesis pass · forward-looking unresolved questions
  • A high-resolution cryo-EM or crystal structure of full-length Kir1.1 in open and closed (pH-gated) states is lacking, preventing atomic-level understanding of how pH-sensor histidines, PIP₂ binding, and the L160 steric gate are allosterically coupled.
  • No experimental structure of Kir1.1 has been reported
  • The conformational pathway linking cytoplasmic pH sensors to the transmembrane gate is modeled but not structurally resolved
  • How dietary K⁺ sensing is transduced to the WNK-SPAK-ROMK axis at the molecular level remains undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005215 transporter activity 5
Localization
GO:0005886 plasma membrane 7
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-382551 Transport of small molecules 3
Partners
AKAP79CFTRITSN1NHERF1NHERF2POSHWNK1WNK4

Evidence

Reading pass · 40 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 ROMK1 channel activity is regulated by phosphorylation/dephosphorylation: channel rundown involves a Mg2+-dependent dephosphorylation process, and PKA-dependent phosphorylation restores and increases channel open probability. Addition of exogenous PKA catalytic subunit increased open probability, and the specific PKA inhibitor PKI partially reversed this effect. Patch clamp (excised inside-out patches), pharmacological inhibitors (okadaic acid, calyculin A, orthovanadate), exogenous PKA catalytic subunit application Proceedings of the National Academy of Sciences of the United States of America High 8058760
1999 PKA activates ROMK1 channels by enhancing their interaction with membrane PIP2: PKA phosphorylation lowers the PIP2 concentration required for channel activation, and mutation of PKA phosphorylation sites decreases PIP2-channel interaction. PKA does not directly activate ROMK1 in membranes devoid of PIP2. Inside-out patch clamp, solution-binding assays with anti-PIP2 antibodies, ATP[gammaS] as PKA substrate, site-directed mutagenesis of PKA sites Proceedings of the National Academy of Sciences of the United States of America High 10318968
2007 WNK1 and WNK4 stimulate clathrin-dependent endocytosis of ROMK1 by interacting with the endocytic scaffold protein intersectin (ITSN) via proline-rich motifs; kinase activity is not required. Disease-causing WNK4 mutations enhance interactions with both ITSN and ROMK1, increasing ROMK1 endocytosis. Co-immunoprecipitation, surface expression assays, endocytosis assays in heterologous cells, mutagenesis of proline-rich motifs The Journal of clinical investigation High 17380208
2002 SGK1 and NHERF2 synergize to stimulate ROMK1 activity by increasing channel abundance in the plasma membrane; neither SGK1 nor NHERF2 alone is sufficient. NHERF2 and SGK1 together decrease channel decay after inhibition of vesicle insertion, indicating enhanced membrane trafficking. Two-electrode voltage clamp in Xenopus oocytes, brefeldin A inhibition of vesicle insertion, surface expression measurement Journal of the American Society of Nephrology : JASN High 12444200
2003 PKC inhibits ROMK1 channel activity by reducing membrane PIP2 content; ROMK1 mutants with reduced PIP2 affinity show increased sensitivity to PKC activation (phorbol ester). After PKC-induced inhibition in cell-attached patches, exogenous PIP2 restores channel activity in excised patches. Cell-attached and inside-out patch clamp in Xenopus oocytes, PIP2 content measurement, PMA/carbachol/calphostin-C pharmacology, mutagenesis The Journal of biological chemistry High 12615924
2000 Protein tyrosine kinase (PTK, c-Src) and protein tyrosine phosphatase (PTP-1D) regulate ROMK1 surface expression: inhibiting PTP increases internalization of ROMK1, while inhibiting PTK stimulates insertion of ROMK1 into the plasma membrane. Tyrosine residue Y337 of ROMK1 is essential for this regulation. PTK inhibition also requires intact microtubules for its exocytic effect. Two-electrode voltage clamp, patch clamp, co-expression of c-Src in Xenopus oocytes, pharmacological inhibitors (PAO, herbimycin A, colchicine, taxol, sucrose/concanavalin A), site-directed mutagenesis (Y337A) The Journal of biological chemistry High 11114300
2001 Inhibition of protein tyrosine phosphatase increases tyrosine phosphorylation of ROMK1 at Y337 and induces dynamin-dependent endocytosis of the channel, reducing surface expression by 65%. Dominant negative dynamin (K44A) completely blocks this endocytic effect. Confocal microscopy of GFP-ROMK1, biotin labeling, patch clamp, co-transfection with c-Src and dominant negative dynamin, mutagenesis (Y337A) The Journal of biological chemistry High 11719519
2002 ROMK1 is a substrate of PKC; serine residues S4 and S201 are the two main PKC phosphorylation sites essential for surface expression of ROMK1. Mutating both sites (S4/201A) reduces surface expression to near-zero; phosphomimetic S4/201D mutation completely restores surface expression and K+ current. In vitro phosphorylation assay with 32P-ATP, site-directed mutagenesis, two-electrode voltage clamp, confocal microscopy of GFP-ROMK1, biotin surface labeling in HEK293 cells The Journal of biological chemistry High 12221079
2005 ROMK1 is monoubiquitinated in native renal tissue; Lys22 is the ubiquitin-binding site. Mutation K22R abolishes ubiquitination and increases surface expression and channel activity without altering biophysical properties, demonstrating monoubiquitination reduces surface expression of ROMK1. Immunoprecipitation from renal cortex, site-directed mutagenesis of all intracellular lysines, two-electrode voltage clamp, confocal microscopy, biotin surface labeling in HEK293 cells Proceedings of the National Academy of Sciences of the United States of America High 15767585
2005 WNK3 inhibits ROMK1 channel activity by reducing plasmalemmal surface expression; this inhibition is independent of WNK3 kinase activity and is mediated by the carboxyl terminus of WNK3. A kinase-inactivating mutation or PHA2-homologous missense mutation in WNK3 enhances inhibition of ROMK1. Two-electrode voltage clamp in Xenopus oocytes, surface expression measurements, kinase-dead and disease mutant constructs The Journal of physiology Medium 16357011
1998 PKA-dependent regulation of ROMK1 channels requires an A kinase anchoring protein (AKAP79/75): ROMK1 alone does not respond to forskolin or cAMP, but co-expression with AKAP79 confers cAMP/PKA responsiveness. Both the membrane-targeting domain and PKAII-binding domain of AKAP are required. Two-electrode voltage clamp and patch clamp in Xenopus oocytes, RII overlay assay on kidney membranes, pharmacological inhibition with H89/PKI Proceedings of the National Academy of Sciences of the United States of America High 9707637
1998 pH-dependent gating of ROMK1 (Kir1.1) involves conformational changes in both N terminus (Cys49) and C terminus (Cys308): both intracellular cysteines react with thiol reagents only in the closed (acidified) state, not in the open state, indicating protein domain movement during pH gating. Site-directed mutagenesis of all intracellular cysteines, state-dependent modification by water-soluble oxidants and sulfhydryl reagents, patch clamp The Journal of biological chemistry High 9852128
1996 ROMK1 (Kir1.1) is regulated allosterically by both extracellular K+ concentration and intracellular pH. K+ regulation is determined by the core channel region (M1, M2, P), while pH coupling is determined by the N terminus, as shown by chimeric channel studies exchanging N-termini between ROMK1 and pH-insensitive IRK1. Site-directed mutagenesis, chimeric channel construction, two-electrode voltage clamp in Xenopus oocytes The Journal of biological chemistry High 8663367
1995 The second transmembrane segment (M2) of ROMK1 is a straight alpha-helix with three distinct structural environments: lipid-facing (tolerant to both Trp and Ala), protein-interior-facing (tolerant to Ala only), and pore-facing (intolerant to either substitution), established by systematic perturbation scanning mutagenesis. Site-directed mutagenesis of 18 consecutive M2 residues with Trp and Ala substitutions, functional expression in Xenopus oocytes Proceedings of the National Academy of Sciences of the United States of America High 8618841
2000 Multiple histidine residues in the C terminus of ROMK1 (His225, His274, His342, His354) contribute to CO2 and pH sensing; mutation of each reduces CO2 and pH sensitivity by 20-50%, and simultaneous mutation of all four eliminates CO2 sensitivity. Systematic site-directed mutagenesis of all histidine residues, patch clamp in Xenopus oocytes, CO2 and pH sensitivity measurements The Journal of biological chemistry High 10713095
2005 The pH gate of Kir1.1 is located at the helix bundle crossing near the cytoplasmic end of the inner transmembrane helices: Leu160 residues from each subunit form a steric gate. Replacing L160 with glycine abolishes pH gating; polar substitutions (L160S, L160T) also eliminate gating, indicating size and hydrophobicity at this position are both required. Site-directed mutagenesis, patch clamp in Xenopus oocytes, homology modeling based on KirBac1.1 crystal structure Biophysical journal High 15653740
2006 Cysteine-scanning mutagenesis localizes the Kir1.1 pH gate to the transmembrane pore at position 175: a reintroduced cysteine at M2 position 175 is accessible to MTS reagents in the open state but protected from modification upon channel closure by low pH, indicating a conformational change that occludes the transmembrane pore. Cysteine-scanning mutagenesis, cytoplasmic-side MTS reagent modification (MTSEA, MTSET, MTSES, Ag+) in inside-out macropatches from Xenopus oocytes Biophysical journal High 16891366
2002 The ATP/PIP2 binding site in Kir1.1 is localized to a 39-amino acid region at the proximal C terminus; three conserved arginine residues (R188, R203, R217) are critical for nucleotide binding, and PIP2 competes with ATP at this site. MBP fusion protein binding assay with TNP-ATP fluorescent nucleotide, PIP2 competition assay, site-directed mutagenesis of arginine residues The Journal of biological chemistry High 12381730
2006 CFTR is required for ATP and glibenclamide sensitivity of the 30 pS Kir1.1 channel in TAL cells; both sensitivities are absent in CFTR knockout and deltaF508 mice. PKA activity abrogates the CFTR effect on ATP sensitivity, indicating CFTR provides a PKA-regulated switch determining the ratio of open to ATP-inhibited ROMK channels. Patch clamp in native TAL cells from CFTR knockout and deltaF508 mice, curcumin rescue experiment, PKA manipulation The Journal of clinical investigation High 16470247
2002 ENaC up-regulates Kir1.1 (ROMK1) surface expression and currents, but only in the presence of CFTR; CFTR provides a mechanistic link for coordinated regulation of ENaC and ROMK1. SUR2B does not traffic to the plasma membrane when co-expressed with Kir1.1b. Two-electrode voltage clamp in Xenopus oocytes, surface expression analysis, co-expression of ENaC, CFTR, and Kir1.1 in various combinations The Journal of biological chemistry Medium 11994290
2003 SGK1 stimulates ROMK1 via phosphorylation at Ser44, which shifts the pH sensitivity of the channel to more acidic values; deletion of either the second PDZ domain of NHERF2 or the PDZ binding motif on ROMK1 abolishes the stimulatory effect of SGK1 on ROMK1 surface expression. SGK1 interacts with NHERF2 through the second PDZ domain of NHERF2. Pull-down assays, site-directed mutagenesis of Ser44, two-electrode voltage clamp in Xenopus oocytes, chemiluminescence surface expression assay Biochemical and biophysical research communications Medium 12878206 14623317
2009 POSH acts as an E3 ubiquitin ligase for ROMK1: POSH binds ROMK1 at its N terminus, stimulates ROMK1 ubiquitination (confirmed by in vitro ubiquitination assay), and promotes dynamin-dependent but clathrin-independent endocytosis of ROMK1. Deletion of the RING domain abolishes both ubiquitination and endocytic effects. Immunostaining, Co-IP, GST pulldown, electrophysiology, biotin surface labeling, in vitro ubiquitination assay, dominant-negative dynamin, RING domain deletion The Journal of biological chemistry High 19710010
2004 c-Src (Src family PTK) is co-expressed with ROMK in the TAL, CCD, and OMCD. Stimulation of PTK by phenylarsine oxide in CCD from high-K diet rats decreases ROMK apical/subapical membrane staining and increases intracellular staining, demonstrating PTK controls ROMK membrane localization in the CCD but not the TAL. Immunofluorescence staining, confocal microscopy, biotin labeling, dietary K manipulation in rats American journal of physiology. Renal physiology Medium 15075184
2001 SNARE proteins mediate PTK inhibition-induced exocytosis of ROMK1: tetanus toxin abolishes the herbimycin A-induced increase in surface ROMK1 channels, demonstrating SNARE-dependent exocytosis. Tyrosine dephosphorylation at Y337 is required for this exocytic insertion. Confocal microscopy, patch clamp, biotin surface labeling in HEK293 cells, tetanus toxin treatment, mutagenesis (Y337A) American journal of physiology. Renal physiology Medium 12556363
2008 WNK1 inhibits ROMK1 through its N-terminal proline-rich domain (aa 1-119); an N-linker domain (aa 120-220) antagonizes this inhibition; the kinase domain reverses the N-linker antagonism via charge-charge interactions between K233 and D368 (not kinase activity); the autoinhibitory domain and first coiled-coil domain further modulate the effect through intramolecular interactions. Domain deletion and mutagenesis of WNK1, two-electrode voltage clamp in Xenopus oocytes American journal of physiology. Renal physiology Medium 18550644
2010 Angiotensin II inhibits ROMK1 channels by two mechanisms: (1) PKC-stimulated c-Src tyrosine phosphorylation of ROMK1 at Y337, and (2) synergizing WNK4-mediated inhibition via a PTK-dependent pathway. Losartan or PKC inhibition blocks the effect; the Y337A ROMK1 mutant is resistant to direct Ang II inhibition but not to WNK4-mediated inhibition restored by Ang II. Perforated whole-cell patch clamp in HEK293 cells, Western blot for tyrosine phosphorylation, pharmacological inhibitors (losartan, PKC inhibitor, PTK inhibitor), mutagenesis (Y337A), native CCD patch clamp in rats Kidney international Medium 20927043
2015 WNK4 is a substrate of c-Src at Y1092, Y1094, and Y1143; c-Src and PTP-1D co-immunoprecipitate with WNK4. Phosphorylation at Y1092/Y1094 is required for WNK4-mediated inhibition of ROMK; phosphorylation at Y1143 is required for PTP-1D association and for SGK1 to reverse WNK4 inhibition of ROMK. Western blot, mass spectrometry, co-immunoprecipitation, site-directed mutagenesis of WNK4 tyrosines, functional ROMK assay Proceedings of the National Academy of Sciences of the United States of America High 25805816
2014 SPAK and OSR1 kinases reduce ROMK1 activity and membrane abundance in a catalytic activity-dependent manner: constitutively active SPAK (T233E) and OSR1 (T185E) reduce ROMK1 surface expression, while catalytically inactive mutants (D212A-SPAK, D164A-OSR1) have no effect. Dual electrode voltage clamp and chemiluminescence surface expression assay in Xenopus oocytes, constitutively active and kinase-dead mutants of SPAK and OSR1 Kidney & blood pressure research Medium 25322850
2001 An 'IRA' amino acid triplet in the N-terminal extension of ROMK1 (positions 13-19) blocks interaction with SUR2B, preventing SUR2B from conferring glibenclamide sensitivity. Direct physical interaction between ROMK1 and SUR2B (demonstrated by in vitro co-translation and co-immunoprecipitation) is required for glibenclamide-sensitive K+ currents. N-terminal deletion and substitution mutagenesis of ROMK1, two-electrode voltage clamp in Xenopus oocytes, in vitro co-translation and co-immunoprecipitation The Journal of biological chemistry High 11567030
1998 The NH2 terminus of ROMK1 (specifically serine-4) determines sensitivity to arachidonic acid (AA) inhibition. ROMK2 and ROMK3 splice variants lacking this N-terminal region show minimal AA inhibition; deletion of residues 2-37 or S4A mutation markedly reduces AA-induced inhibition. PKC phosphorylation at S4 also inhibits ROMK1. Patch clamp in Xenopus oocytes, NH2-terminal deletion and point mutagenesis, pharmacological inhibitors (calphostin C, chelerythrine, staurosporine) The American journal of physiology Medium 9458837
1999 A Bartter syndrome-causing truncation mutation (Kir1.1a 331X) reaches the plasma membrane but locks the channel in a closed state. Co-expression with wild-type exerts a dominant negative effect; the extreme C terminus (residues 332-351) is an essential subunit interaction domain controlling oligomerization efficiency and open-state occupancy. Co-expression with wild-type in Xenopus oocytes, GFP fusion for plasma membrane localization, incremental C-terminal reconstruction, tetrameric concatemer approach, patch clamp The Journal of general physiology High 10532965
2009 The immunoglobulin-like domain (IgLD) in the intracellular region of Kir1.1 is essential for thermodynamic stability, trafficking, and gating. Two Bartter syndrome mutations (A198T, Y314C) within the IgLD core impair channel biosynthesis and trafficking; channels that reach the surface are electrically silent due to helix-bundle gate closure and cannot rectify. Atomic model mapping of ABS mutations, thermodynamic stability calculations by computational mutagenesis, mammalian cell trafficking assay, patch clamp electrophysiology, compensatory mutation rescue Channels (Austin, Tex.) Medium 19221509
2009 An intersubunit salt bridge (R128-E132) in the P-loop near the selectivity filter stabilizes the active state of Kir1.1. Disruption of this salt bridge causes inactivation even in 100 mM external K+; external Ba2+ or tertiapin-Q binding to the outer channel mouth prevents inactivation, indicating inactivation involves conformational changes near the selectivity filter analogous to C-type inactivation. Site-directed mutagenesis, two-electrode voltage clamp in Xenopus oocytes, external Ba2+ and tertiapin-Q pharmacology, variable external K+ manipulation Biophysical journal Medium 19686653
2011 High-K diet causes a large increase in apical ROMK expression in DCT2, CNT, and CD but not DCT1, accompanied by dramatically increased mature glycosylation, demonstrating dietary K+ regulates ROMK1 surface density through altered trafficking and glycosylation in a nephron-segment-specific manner. Immunofluorescence with new ROMK-specific antibodies verified on knockout mice, segmental markers, glycosylation state analysis by Western blot, dietary K manipulation American journal of physiology. Renal physiology High 21454252
2016 ROMK1 isoform-specific knockout mice (Romk1-/-) do not develop Bartter phenotype (no reduced NKCC2 activity or increased NCC), indicating no functional link between ROMK1 and NKCC2 in TAL. However, high K+ diet-stimulated K+ secretion in the collecting tubule is absent in Romk1-/-, demonstrating ROMK1 is specifically required for dietary K+-induced K+ secretion. ES cell Cre-LoxP selective deletion of Romk1-specific exon 1, patch clamp of collecting tubule SK channels, immunofluorescence, dietary K manipulation, comparison with global Romk-/- knockout The Journal of biological chemistry High 26728465
2014 Kir1.1 (ROMK) channels are required for gastric acid secretion and co-localize with the beta-subunit of H+/K+-ATPase in gastric parietal cells. In Kir1.1-deficient mice, secretagogue-stimulated acid secretion is absent; luminal K+ restores acid secretion, demonstrating Kir1.1 provides a K+ recycling pathway essential for H+/K+-ATPase function in parietal cells. Kir1.1 knockout mice, immunofluorescence co-localization, whole-stomach acid secretion, perfused gastric gland secretion assay, luminal tertiapin-Q and XE991 inhibition Pflugers Archiv : European journal of physiology High 25127675
2017 Small-molecule inhibitor VU590 blocks Kir1.1 within the pore in a voltage- and K+-dependent manner; asparagine N171 is the only pore-lining residue required for high-affinity block, and negatively charged substitutions (N171D/E) weaken block, while equivalent negative charge in Kir7.1 enhances block, revealing differential roles of pore polarity in determining inhibitor pharmacology. Molecular modeling, site-directed mutagenesis, patch clamp electrophysiology Molecular pharmacology Medium 28619748
2009 FRET measurements show that during pHi gating of Kir1.1, the cytoplasmic pore conformation changes: N- and C-termini move apart from each other when the channel is open (high pH), and move closer when closed (low pH). FRET with ECFP-Kir1.1-EYFP fusion constructs, pH manipulation in Xenopus oocytes Journal of biomedical science Medium 19272129
2017 NHERF1 knockdown in M-1 CCD cells reduces surface expression of ROMK1 (detected by biotin labeling) and decreases Ba2+-sensitive whole-cell K+ current and the number of active channels in patches, demonstrating NHERF1 is required for ROMK1 surface expression and function in native collecting duct cells. NHERF1 siRNA knockdown in M-1 cells, cell surface biotinylation assay, patch clamp electrophysiology, transfection with EGFP-ROMK1 Biochemical and biophysical research communications Medium 28533091
1994 Human ROMK1 gene produces multiple transcript isoforms (ROMK1A, 1B, 1C) through alternative splicing and use of multiple promoters from a single locus at chromosome 11q24. ROMK1A encodes a functional Ba2+-sensitive inwardly rectifying K+ channel when expressed in Xenopus oocytes. cDNA cloning, RT-PCR, alternative splicing analysis, fluorescence in situ hybridization, Xenopus oocyte expression and two-electrode voltage clamp Molecular pharmacology High 8190102

Source papers

Stage 0 corpus · 96 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1994 Regulation of ROMK1 K+ channel activity involves phosphorylation processes. Proceedings of the National Academy of Sciences of the United States of America 132 8058760
1999 Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism. Proceedings of the National Academy of Sciences of the United States of America 126 10318968
2007 Intersectin links WNK kinases to endocytosis of ROMK1. The Journal of clinical investigation 119 17380208
2002 The serum and glucocorticoid-inducible kinase SGK1 and the Na+/H+ exchange regulating factor NHERF2 synergize to stimulate the renal outer medullary K+ channel ROMK1. Journal of the American Society of Nephrology : JASN 105 12444200
2011 Differential regulation of ROMK (Kir1.1) in distal nephron segments by dietary potassium. American journal of physiology. Renal physiology 92 21454252
2000 ROMK1 (Kir1.1) causes apoptosis and chronic silencing of hippocampal neurons. Journal of neurophysiology 87 10938328
1998 pH-dependent gating of ROMK (Kir1.1) channels involves conformational changes in both N and C termini. The Journal of biological chemistry 72 9852128
1996 Extracellular K+ and intracellular pH allosterically regulate renal Kir1.1 channels. The Journal of biological chemistry 65 8663367
2006 Regulation of ROMK (Kir1.1) channels: new mechanisms and aspects. American journal of physiology. Renal physiology 58 16339961
2003 Protein kinase C inhibits ROMK1 channel activity via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism. The Journal of biological chemistry 58 12615924
2000 Regulation of ROMK1 channels by protein-tyrosine kinase and -tyrosine phosphatase. The Journal of biological chemistry 54 11114300
2002 Protein kinase C (PKC)-induced phosphorylation of ROMK1 is essential for the surface expression of ROMK1 channels. The Journal of biological chemistry 52 12221079
2005 WNK3, a kinase related to genes mutated in hereditary hypertension with hyperkalaemia, regulates the K+ channel ROMK1 (Kir1.1). The Journal of physiology 51 16357011
2004 Protein tyrosine kinase is expressed and regulates ROMK1 location in the cortical collecting duct. American journal of physiology. Renal physiology 51 15075184
2001 Inhibition of protein-tyrosine phosphatase stimulates the dynamin-dependent endocytosis of ROMK1. The Journal of biological chemistry 51 11719519
1996 Imaging ROMK1 inwardly rectifying ATP-sensitive K+ channel protein using atomic force microscopy. Proceedings of the National Academy of Sciences of the United States of America 51 8710944
1998 The A kinase anchoring protein is required for mediating the effect of protein kinase A on ROMK1 channels. Proceedings of the National Academy of Sciences of the United States of America 50 9707637
2006 CFTR is required for PKA-regulated ATP sensitivity of Kir1.1 potassium channels in mouse kidney. The Journal of clinical investigation 49 16470247
1994 Alternative splicing of human inwardly rectifying K+ channel ROMK1 mRNA. Molecular pharmacology 49 8190102
2003 Molecular requirements for the regulation of the renal outer medullary K(+) channel ROMK1 by the serum- and glucocorticoid-inducible kinase SGK1. Biochemical and biophysical research communications 47 14623317
2000 Involvement of histidine residues in proton sensing of ROMK1 channel. The Journal of biological chemistry 46 10713095
2005 ROMK1 channel activity is regulated by monoubiquitination. Proceedings of the National Academy of Sciences of the United States of America 43 15767585
1999 A mutation linked with Bartter's syndrome locks Kir 1.1a (ROMK1) channels in a closed state. The Journal of general physiology 41 10532965
2002 Cystic fibrosis transmembrane conductance regulator-dependent up-regulation of Kir1.1 (ROMK) renal K+ channels by the epithelial sodium channel. The Journal of biological chemistry 40 11994290
2010 Angiotensin II diminishes the effect of SGK1 on the WNK4-mediated inhibition of ROMK1 channels. Kidney international 39 20927043
1995 Three distinct structural environments of a transmembrane domain in the inwardly rectifying potassium channel ROMK1 defined by perturbation. Proceedings of the National Academy of Sciences of the United States of America 39 8618841
2003 Negative charge at the consensus sequence for the serum- and glucocorticoid-inducible kinase, SGK1, determines pH sensitivity of the renal outer medullary K+ channel, ROMK1. Biochemical and biophysical research communications 32 12878206
2005 Structural locus of the pH gate in the Kir1.1 inward rectifier channel. Biophysical journal 31 15653740
2000 Molecular determinants for the distinct pH sensitivity of Kir1.1 and Kir4.1 channels. American journal of physiology. Cell physiology 30 11029294
2011 Functional and developmental expression of a zebrafish Kir1.1 (ROMK) potassium channel homologue Kcnj1. The Journal of physiology 29 21262879
2000 A single residue contributes to the difference between Kir4.1 and Kir1.1 channels in pH sensitivity, rectification and single channel conductance. The Journal of physiology 27 11034617
1994 Differential expression of the inwardly-rectifying K-channel ROMK1 in rat brain. Brain research. Molecular brain research 26 7968375
2010 Hypertension resistance polymorphisms in ROMK (Kir1.1) alter channel function by different mechanisms. American journal of physiology. Renal physiology 25 20926634
2009 The Kir channel immunoglobulin domain is essential for Kir1.1 (ROMK) thermodynamic stability, trafficking and gating. Channels (Austin, Tex.) 25 19221509
2009 POSH stimulates the ubiquitination and the clathrin-independent endocytosis of ROMK1 channels. The Journal of biological chemistry 25 19710010
2002 Intrinsic sensitivity of Kir1.1 (ROMK) to glibenclamide in the absence of SUR2B. Implications for the identity of the renal ATP-regulated secretory K+ channel. The Journal of biological chemistry 25 11927600
2002 Localization of the ATP/phosphatidylinositol 4,5 diphosphate-binding site to a 39-amino acid region of the carboxyl terminus of the ATP-regulated K+ channel Kir1.1. The Journal of biological chemistry 24 12381730
2000 Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function. The Journal of biological chemistry 24 10889209
2014 SPAK and OSR1 dependent down-regulation of murine renal outer medullary K channel ROMK1. Kidney & blood pressure research 23 25322850
2008 Domains of WNK1 kinase in the regulation of ROMK1. American journal of physiology. Renal physiology 21 18550644
1998 Role of the NH2 terminus of the cloned renal K+ channel, ROMK1, in arachidonic acid-mediated inhibition. The American journal of physiology 21 9458837
1998 A hyperprostaglandin E syndrome mutation in Kir1.1 (renal outer medullary potassium) channels reveals a crucial residue for channel function in Kir1.3 channels. The Journal of biological chemistry 21 9727001
2006 Localization of the pH gate in Kir1.1 channels. Biophysical journal 20 16891366
2006 Characterization of Kir1.1 channels with the use of a radiolabeled derivative of tertiapin. Biochemistry 20 16906771
2001 An amino acid triplet in the NH2 terminus of rat ROMK1 determines interaction with SUR2B. The Journal of biological chemistry 20 11567030
2008 PKA-mediated phosphorylation is a novel mechanism for levetiracetam, an antiepileptic drug, activating ROMK1 channels. Biochemical pharmacology 19 18547545
1998 Large deletion of the 5' end of the ROMK1 gene causes antenatal Bartter syndrome. Journal of the American Society of Nephrology : JASN 19 9848791
2015 Src-family protein tyrosine kinase phosphorylates WNK4 and modulates its inhibitory effect on KCNJ1 (ROMK). Proceedings of the National Academy of Sciences of the United States of America 18 25805816
2012 The inwardly rectifying potassium channel Kir1.1: development of functional assays to identify and characterize channel inhibitors. Assay and drug development technologies 17 22881347
2006 Role of conserved glycines in pH gating of Kir1.1 (ROMK). Biophysical journal 17 16533837
1997 Structural activity of a cloned potassium channel (ROMK1) monitored with the atomic force microscope: the "molecular-sandwich" technique. Proceedings of the National Academy of Sciences of the United States of America 16 9391167
2009 An intersubunit salt bridge near the selectivity filter stabilizes the active state of Kir1.1. Biophysical journal 15 19686653
1997 Nucleotide sequence analysis of the human KCNJ1 potassium channel locus. Gene 15 9099852
2017 Pore Polarity and Charge Determine Differential Block of Kir1.1 and Kir7.1 Potassium Channels by Small-Molecule Inhibitor VU590. Molecular pharmacology 14 28619748
2002 Tetanus toxin abolishes exocytosis of ROMK1 induced by inhibition of protein tyrosine kinase. American journal of physiology. Renal physiology 13 12556363
1998 Secondary structure analysis of the putative membrane-associated domains of the inward rectifier K+ channel ROMK1. The Biochemical journal 13 9761737
2020 Late-Onset Bartter Syndrome Type II Due to a Homozygous Mutation in KCNJ1 Gene: A Case Report and Literature Review. The American journal of case reports 12 32997650
2016 Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion. The Journal of biological chemistry 12 26728465
2007 A novel mutation in KCNJ1 in a Bartter syndrome case diagnosed as pseudohypoaldosteronism. Pediatric nephrology (Berlin, Germany) 12 17401586
2001 PKA-induced stimulation of ROMK1 channel activity is governed by both tethering and non-tethering domains of an A kinase anchor protein. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 12 11410709
2019 A novel compound heterozygous KCNJ1 gene mutation presenting as late-onset Bartter syndrome: Case report. Medicine 11 31441846
2013 Identification of compound heterozygous KCNJ1 mutations (encoding ROMK) in a kindred with Bartter's syndrome and a functional analysis of their pathogenicity. Physiological reports 11 24400161
2007 Charges in the cytoplasmic pore control intrinsic inward rectification and single-channel properties in Kir1.1 and Kir2.1 channels. The Journal of membrane biology 11 17568976
2000 A Bartter's syndrome mutation of ROMK1 exerts dominant negative effects on K(+) conductance. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 11 10878442
1999 The effects of oxidizing and cysteine-reactive reagents on the inward rectifier potassium channels Kir2.3 and Kir1.1. Pflugers Archiv : European journal of physiology 11 10591077
1998 Probing the water permeability of ROMK1 and amphotericin B channels using Xenopus oocytes. Biochimica et biophysica acta 11 9459580
2007 External K activation of Kir1.1 depends on the pH gate. Biophysical journal 10 17496015
2004 Potassium-dependent slow inactivation of Kir1.1 (ROMK) channels. Biophysical journal 10 15041655
1997 Mapping the kidney potassium channel ROMK1. Glycosylation of the pore signature sequence and the COOH terminus. The Journal of biological chemistry 10 9312136
2014 Kir1.1 (ROMK) and Kv7.1 (KCNQ1/KvLQT1) are essential for normal gastric acid secretion: importance of functional Kir1.1. Pflugers Archiv : European journal of physiology 9 25127675
2020 Eight novel KCNJ1 variants and parathyroid hormone overaction or resistance in 5 probands with Bartter syndrome type 2. Clinica chimica acta; international journal of clinical chemistry 8 33058840
2010 A conserved arginine near the filter of Kir1.1 controls Rb/K selectivity. Channels (Austin, Tex.) 8 20458182
2022 Late-Onset Bartter Syndrome Type II Due to a Novel Compound Heterozygous Mutation in KCNJ1 Gene: A Case Report and Literature Review. Frontiers in medicine 7 35463019
2008 Gabapentin activates ROMK1 channels by a protein kinase A (PKA)-dependent mechanism. British journal of pharmacology 7 18311184
1999 Processing and transport of ROMK1 channel is temperature-sensitive. Biochemical and biophysical research communications 7 10425191
2019 Polymorphisms in PCSK9, LDLR, BCMO1, SLC12A3, and KCNJ1 are Associated with Serum Lipid Profile in Chinese Han Population. International journal of environmental research and public health 6 31480784
2011 Protein kinase C mediated pH(i)-regulation of ROMK1 channels via a phosphatidylinositol-4,5-bisphosphate-dependent mechanism. Journal of molecular modeling 6 22139477
2005 Subunit stoichiometry of the Kir1.1 channel in proton-dependent gating. The Journal of biological chemistry 5 15691840
2015 Direct injection of cell-free Kir1.1 protein into Xenopus oocytes replicates single-channel currents derived from Kir1.1 mRNA. Channels (Austin, Tex.) 4 26102359
2014 Pregabalin activates ROMK1 channels via cAMP-dependent protein kinase and protein kinase C. European journal of pharmacology 4 25008072
2008 Functional and structural characterization of PKA-mediated pHi gating of ROMK1 channels. Journal of molecular graphics & modelling 4 18620882
2022 A novel mutation of KCNJ1 identified in an affected child with nephrolithiasis. BMC nephrology 3 35761198
2009 Structural changes in the cytoplasmic pore of the Kir1.1 channel during pHi-gating probed by FRET. Journal of biomedical science 3 19272129
2007 Moving the pH gate of the Kir1.1 inward rectifier channel. Channels (Austin, Tex.) 3 19170254
1999 Na(+) sensitivity of ROMK1 K(+) channel: role of the Na(+)/H(+) antiporter. The Journal of membrane biology 3 10552015
2023 Association of polymorphisms of calcium reabsorption genes SLC12A1, KCNJ1 and SLC8A1 with colorectal adenoma. Journal of cancer research and clinical oncology 2 37074453
2022 Late-Onset Bartter's Syndrome Type II with End-Stage Renal Disease Due to a Novel Mutation in KCNJ1 Gene in an Indian Adult Male - A Case Report. Indian journal of nephrology 1 37197039
2021 Antenatal Bartter syndrome: a new compound heterozygous mutation in exon 2 of KCNJ1 gene. BMJ case reports 1 34663630
2017 Na+/H+ exchange regulatory factor 1 is required for ROMK1 K+ channel expression in the surface membrane of cultured M-1 cortical collecting duct cells. Biochemical and biophysical research communications 1 28533091
2017 [A clinical and hereditary analysis of novel complex heterozygous KCNJ1 mutation in a Bartter syndrome type Ⅱ patient]. Zhonghua nei ke za zhi 1 29036958
2003 Kir1.1 expression in embryonic kidney epithelia. Biochemical and biophysical research communications 1 14651999
2001 Biophysical effects of pore mutations of ROMK1. Clinical science (London, England : 1979) 1 11473485
2025 Case Report: Type II Bartter syndrome with a novel KCNJ1 variant in a premature neonate presenting with features of salt-wasting congenital adrenal crisis and pseudo-hypoaldosteronism. Frontiers in pediatrics 0 40630717
2025 Novel Compound Heterozygous Mutation in the KCNJ1 Gene Causes Bartter Syndrome. Nephrology (Carlton, Vic.) 0 41069163
2017 [The role of estrogen related-receptor γ and ATP-dependent K(+) channel Kcnj1 in renal ischemia-reperfusion injury]. Zhonghua yi xue za zhi 0 29061011
2001 [Neonatal Bartter disease diagnosed with the detection of a mutation of the KCNJ1 gene which codifies the synthesis of the renal ROMK1 potassium channel]. Nefrologia : publicacion oficial de la Sociedad Espanola Nefrologia 0 11795013