Component
ROMK2 splice isoform
ROMK2 isoform of KCNJ1 studied by Yang et al.; rat channel expressed in Xenopus oocytes.
3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
Extracellular Mg2+ also reduced ROMK2 single-channel current, with stronger apparent block as external K+ fell.
Experimental context and source evidence
- cross_nutrient
- magnesium -> potassium
- experimental_model
- Heterologous channel expression and patch-clamp
- limitations
- Excised-patch channel behavior does not quantify whole-body potassium loss in humans.
- magnesium-pool
- Extracellular free Mg2+
- nutrient_topic
- Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
- organism
- Xenopus laevis host; mammalian ROMK channel
- plain_language
- Mg on the urine-facing side can also limit channel current; its action is separate from intracellular Mg.
- primary_references
- [yang-2010-romk-magnesium] Magnesium modulates ROMK channel-mediated potassium secretion (2010). https://pubmed.ncbi.nlm.nih.gov/21030597/ DOI: 10.1681/ASN.2010060617
- tissue_or_cell_type
- Oocyte membrane
Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 141–152
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Heterologous channel expression and patch-clamp · source_derived_draft · unverified_draft
### mg-extracellular-romk2-block Extracellular Mg2+ also reduced ROMK2 single-channel current, with stronger apparent block as external K+ fell. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Mg on the urine-facing side can also limit channel current; its action is separate from intracellular Mg. organism: Xenopus laevis host; mammalian ROMK channel tissue_or_cell_type: Oocyte membrane experimental_model: Heterologous channel expression and patch-clamp limitations: Excised-patch channel behavior does not quantify whole-body potassium loss in humans. cross_nutrient: magnesium -> potassium magnesium-pool: Extracellular free Mg2+ [yang-2010-romk-magnesium] Magnesium modulates ROMK channel-mediated potassium secretion (2010). https://pubmed.ncbi.nlm.nih.gov/21030597/ DOI: 10.1681/ASN.2010060617
Complete structured claim and evidenceLower external K+ increased the apparent affinity of cytoplasmic Mg2+ block of rat ROMK2 and permitted block over physiologically relevant negative voltages.
Experimental context and source evidence
- cross_nutrient
- magnesium -> potassium
- experimental_model
- Heterologous channel expression and patch-clamp
- exposure
- External K tested at 110, 11 and 1.1 mM; experimental concentrations, not dietary targets.
- limitations
- Excised-patch channel behavior does not quantify whole-body potassium loss in humans.
- nutrient_topic
- Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
- organism
- Xenopus laevis host; mammalian ROMK channel
- plain_language
- The potassium concentration outside the cell changes how strongly inside Mg restrains potassium exit.
- primary_references
- [yang-2010-romk-magnesium] Magnesium modulates ROMK channel-mediated potassium secretion (2010). https://pubmed.ncbi.nlm.nih.gov/21030597/ DOI: 10.1681/ASN.2010060617
- tissue_or_cell_type
- Oocyte membrane
Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 116–127
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Heterologous channel expression and patch-clamp · source_derived_draft · unverified_draft
### mg-romk2-low-external-k-enhances-block Lower external K+ increased the apparent affinity of cytoplasmic Mg2+ block of rat ROMK2 and permitted block over physiologically relevant negative voltages. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The potassium concentration outside the cell changes how strongly inside Mg restrains potassium exit. organism: Xenopus laevis host; mammalian ROMK channel tissue_or_cell_type: Oocyte membrane experimental_model: Heterologous channel expression and patch-clamp limitations: Excised-patch channel behavior does not quantify whole-body potassium loss in humans. cross_nutrient: magnesium -> potassium exposure: External K tested at 110, 11 and 1.1 mM; experimental concentrations, not dietary targets. [yang-2010-romk-magnesium] Magnesium modulates ROMK channel-mediated potassium secretion (2010). https://pubmed.ncbi.nlm.nih.gov/21030597/ DOI: 10.1681/ASN.2010060617
Complete structured claim and evidence
Where it participates (unsigned role)
Romk1-specific deletion blunted high-K-induced collecting-tubule ROMK surface recruitment and caused hyperkalemia during that challenge.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_location
- Abstract; high-K channel-number and localization comparison.
- experimental_model
- Isoform-specific knockout; high-K diet
- limitations
- Baseline channel gating and NKCC2 phenotype were preserved; not equivalent to pan-ROMK deletion.
- nutrient_topic
- Potassium research collection; topical membership is not evidence of a direct dietary effect. · Potassium
- organism
- Mus musculus
- plain_language
- This ROMK splice isoform helps increase potassium exit-channel availability when intake rises.
- primary_references
- [romk1-2016-isoform] Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4777858/ DOI: 10.1074/jbc.M115.707877
- tissue_or_cell_type
- Collecting tubule
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 344–354
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isoform-specific knockout; high-K diet · source_derived_draft · unverified_draft
### renal-romk1-needed-high-k-adaptation Romk1-specific deletion blunted high-K-induced collecting-tubule ROMK surface recruitment and caused hyperkalemia during that challenge. Condition category: machinery_impairment nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: This ROMK splice isoform helps increase potassium exit-channel availability when intake rises. organism: Mus musculus tissue_or_cell_type: Collecting tubule experimental_model: Isoform-specific knockout; high-K diet limitations: Baseline channel gating and NKCC2 phenotype were preserved; not equivalent to pan-ROMK deletion. evidence_location: Abstract; high-K channel-number and localization comparison. [romk1-2016-isoform] Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion (2016). https://pmc.ncbi.nlm.nih.gov/articles/PMC4777858/ DOI: 10.1074/jbc.M115.707877
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.