ArticleThe Journal of biological chemistry2015
Identification of the Intracellular Na+ Sensor in Slo2.1 Potassium Channels.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Unraveling the mechanisms of slack channel mutations in epileptic disorders.Acta epileptologica · 2026Review
- A molecular switch in RCK2 triggers sodium-dependent activation of KBiophysical journal · 2024Article
- Plant Salinity Sensors: Current Understanding and Future Directions.Frontiers in plant science · 2022Review
- The Epilepsy of Infancy With Migrating Focal Seizures: Identification ofFrontiers in cellular neuroscience · 2020Article
- Oxytocin can regulate myometrial smooth muscle excitability by inhibiting the NaThe Journal of physiology · 2019Article
- Na+ extrusion from the cytosol and tissue-specific Na+ sequestration in roots confer differential salt stress tolerance between durum and bread wheat.Journal of experimental botany · 2018Article
- Cardiac metabolic effects of KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Molecular mechanisms of Slo2 KThe Journal of physiology · 2017Article
- International Union of Basic and Clinical Pharmacology. C. Nomenclature and Properties of Calcium-Activated and Sodium-Activated Potassium Channels.Pharmacological reviews · 2017Review
- Hydrophobic interactions between the S5 segment and the pore helix stabilizes the closed state of Slo2.1 potassium channels.Biochimica et biophysica acta · 2016Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Slo2 potassium channels have a very low open probability under normal physiological conditions, but are readily activated in response to an elevated [Na(+)]i (e.g. during ischemia). An intracellular Na(+) coordination motif (DX(R/K)XXH) was previously identified in Kir3.2, Kir3.4, Kir5.1, and Slo2.2 channel subunits. Based loosely on this sequence, we identified five potential Na(+) coordination motifs in the C terminus of the Slo2.1 subunit. The Asp residue in each sequence was substituted with Arg, and single mutant channels were heterologously expressed in Xenopus oocytes. The Na(+) sensitivity of each of the mutant channels was assessed by voltage clamp of oocytes using micropipettes filled with 2 M NaCl. Wild-type channels and four of the mutant Slo2.1 channels were rapidly activated by leakage of NaCl solution into the cytoplasm. D757R Slo2.1 channels were not activated by NaCl, but were activated by the fenamate niflumic acid, confirming their functional expression. In whole cell voltage clamp recordings of HEK293 cells, wild-type but not D757R Slo2.1 channels were activated by a [NaCl]i of 70 mM. Thus, a single Asp residue can account for the sensitivity of Slo2.1 channels to intracellular Na(+). In excised inside-out macropatches of HEK293 cells, activation of wild-type Slo2.1 currents by 3 mM niflumic acid was 14-fold greater than activation achieved by increasing [NaCl]i from 3 to 100 mM. Thus, relative to fenamates, intracellular Na(+) is a poor activator of Slo2.1.
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