Genomes and Genes
Gene Symbol: Kir5 1
Description: potassium voltage-gated channel subfamily J member 16
Alias: Kir5.1, inward rectifier potassium channel 16, BIR9, inward rectifier K(+) channel Kir5.1, potassium channel, inwardly rectifying subfamily J member 16, potassium inwardly-rectifying channel, subfamily J, member 16
- In vivo formation of a proton-sensitive K+ channel by heteromeric subunit assembly of Kir5.1 with Kir4.1M Tanemoto
Department of Pharmacology II, Graduate School of Medicine, Osaka University, Yamada oka 2 2, Suita, Osaka 565 0871, Japan
J Physiol 525:587-92. 2000..1 with Kir4.1 occurs in vivo, at least in kidney. The heteromeric Kir4. 1/Kir5.1 channel may therefore sense intracellular pH in renal epithelium and be involved in the regulation of acid-base homeostasis...
- Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channelsAngelos Aristeidis Konstas
University Laboratory of Physiology, Oxford, OX1 3PT, United Kingdom
Am J Physiol Cell Physiol 284:C910-7. 2003....
- pH dependence of the inwardly rectifying potassium channel, Kir5.1, and localization in renal tubular epitheliaS J Tucker
University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, United Kingdom
J Biol Chem 275:16404-7. 2000..1 subunit. These findings suggest that Kir5.1/Kir4.1 heteromeric channels are likely to exist in vivo and implicate an important and novel functional role for the Kir5.1 subunit...
- Expression of an inwardly rectifying K+ channel, Kir5.1, in specific types of fibrocytes in the cochlear lateral wall suggests its functional importance in the establishment of endocochlear potentialHiroshi Hibino
Department of Pharmacology II, Graduate School of Medicine, Osaka University, 2 2 Yamada oka, Suita, Osaka, 565 0871, Japan
Eur J Neurosci 19:76-84. 2004..1 and was correlated with the 'rapid' phase of the elevation of endocochlear potential (EP). Kir5.1 and Kir4.1 channel-subunits may therefore play distinct functional roles in K+ circulation in the cochlear lateral wall...
- Astrocytes in the retrotrapezoid nucleus sense H+ by inhibition of a Kir4.1-Kir5.1-like current and may contribute to chemoreception by a purinergic mechanismIan C Wenker
University of Connecticut, Department of Physiology and Neurobiology, 75 N Eagleville Rd, Storrs, CT 06269, USA
J Neurophysiol 104:3042-52. 2010..We conclude that RTN astrocytes sense CO(2)/H(+) in part by inhibition of a Kir4.1-Kir5.1-like current and may provide an excitatory purinergic drive to pH-sensitive neurons...
- Kir5.1 underlies long-lived subconductance levels in heteromeric Kir4.1/Kir5.1 channels from Xenopus tropicalisLijun Shang
Clarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, United Kingdom
Biochem Biophys Res Commun 388:501-5. 2009..These novel channels now provide an excellent model system to determine the structural basis of subconductance levels and contribution of heteromeric pore architecture to this process...
- Cloning and expression of a family of inward rectifier potassium channelsC T Bond
Vollum Institute, Oregon Health Sciences University, Portland 97201
Receptors Channels 2:183-91. 1994..The results demonstrate the existence of a large and widely expressed family of inward rectifier potassium channel subunits with distinct tissue distributions and functional properties...
- PDZ binding motif-dependent localization of K+ channel on the basolateral side in distal tubulesMasayuki Tanemoto
Division of Nephrology, Hypertension and Endocrinology, Department of Medicine, Tohoku University Graduate School of Medicine, 1 1 Seiryo cho, Aoba ku, Sendai 980 8574, Japan
Am J Physiol Renal Physiol 287:F1148-53. 2004..1 was responsible for this intracellular localization. These data suggest the signals on the COOH terminus of Kir4.1, including PDZ binding motif, determine the intracellular localization of Kir5.1/Kir4.1 heteromer in distal tubules...
- Novel nucleotide-binding sites in ATP-sensitive potassium channels formed at gating interfacesKe Dong
Department of Cellular and Molecular Physiology, School of Medicine, Yale University, New Haven, CT, USA
EMBO J 24:1318-29. 2005..The short N- and C-terminal segments comprising the novel intermolecular NBS are next to helices that likely move with channel opening/closing, suggesting a lock-and-key model for ligand gating...