2000
DOI: 10.1085/jgp.116.1.33
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Biophysical and Molecular Mechanisms Underlying the Modulation of Heteromeric Kir4.1–Kir5.1 Channels by Co2 and Ph

Abstract: CO2 chemoreception may be related to modulation of inward rectifier K+ channels (Kir channels) in brainstem neurons. Kir4.1 is expressed predominantly in the brainstem and inhibited during hypercapnia. Although the homomeric Kir4.1 only responds to severe intracellular acidification, coexpression of Kir4.1 with Kir5.1 greatly enhances channel sensitivities to CO2 and pH. To understand the biophysical and molecular mechanisms underlying the modulation of these currents by CO2 and pH, heteromeric Kir4.1–Kir5.1 w… Show more

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Cited by 95 publications
(94 citation statements)
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“…On the other hand, the coexpression of Kir4.1 and Kir5.1 units leads to the formation of a 43-to 60-pS K ϩ channel (34, 49) with an intermediate inward rectification (G in /G out ϳ4) and a P o of ϳ0.4 (49). In addition, channels formed by the Kir4.1/Kir5.1 assemblage are sensitive to pH i changes around the physiological range, with pK values of ϳ7.…”
Section: Molecular Candidates For Basolateral K ϩ Channels In Mouse Cmentioning
confidence: 99%
“…On the other hand, the coexpression of Kir4.1 and Kir5.1 units leads to the formation of a 43-to 60-pS K ϩ channel (34, 49) with an intermediate inward rectification (G in /G out ϳ4) and a P o of ϳ0.4 (49). In addition, channels formed by the Kir4.1/Kir5.1 assemblage are sensitive to pH i changes around the physiological range, with pK values of ϳ7.…”
Section: Molecular Candidates For Basolateral K ϩ Channels In Mouse Cmentioning
confidence: 99%
“…Modulation of ROMK (Kir1.1; KCNJ1) via alkalinization increases P o by decreasing the number of long-duration closures without changing open durations (9,36). Heteromeric Kir4.1-Kir5.1 (KCNJ10-KCNJ16) also increases P o upon alkalinization through a loss of long-duration closures (59). Stimulation of IK1 (KCNN4) by the K ϩ channel opener 1-EBIO occurs through a decrease in long closed durations without any change in open durations (48).…”
Section: Continued CLmentioning
confidence: 99%
“…Drawing analogy to pH-sensitive gating of potassium channels (Schulte and Fakler, 2000;Yang et al, 2000), we hypothesized that the molecular determinants for the proton site are localized near the extracellular end of the M3 transmembrane domain of NMDA receptors that contains the lurcher motif (SYTANLAAF). The lurcher motif is conserved in all glutamate receptors and is thought to play a critical role in gating (Kohda et al, 2000;Taverna et al, 2000;Jones et al, 2002).…”
mentioning
confidence: 99%