Inwardly rectifying potassium channels (KIR) in GtoPdb v.2021.3 [PDF]
The 2TM domain family of K channels are also known as the inward-rectifier K channel family. This family includes the strong inward-rectifier K channels (Kir2.x) that are constitutively active, the G-protein-activated inward-rectifier K channels (Kir3.x)
Adelman, John P. +17 more
core +3 more sources
pH Dependence of the Inwardly Rectifying Potassium Channel, Kir5.1, and Localization in Renal Tubular Epithelia [PDF]
The physiological role of the inwardly rectifying potassium channel, Kir5.1, is poorly understood, as is the molecular identity of many renal potassium channels. In this study we have used Kir5.1-specific antibodies to reveal abundant expression of Kir5.1 in renal tubular epithelial cells, where Kir4.1 is also expressed.
TUCKER J. S. +4 more
openaire +5 more sources
Parkinson's disease‐linked Kir4.2 mutation R28C leads to loss of ion channel function
Abstract figure legend Pathogenic impact of the PD‐linked Kir4.2R28C mutation on Kir4.2 channel proteostasis and function. The Kir4.2R28C mutation, identified in a familial Parkinson's disease (PD) pedigree, leads to a near‐complete loss of potassium channel function and exerts a significant dominant‐negative effect.
Xiaoyi Chen +8 more
wiley +1 more source
Formation of Functional Heterodimers by TREK-1 and TREK-2 Two-pore Domain Potassium Channel Subunits. [PDF]
Two-pore domain (K2P) potassium channels are the major molecular correlates of the background (leak) K+ current in a wide variety of cell types. They generally play a key role in setting the resting membrane potential and regulate the response of ...
Czirják Gábor +2 more
core +1 more source
Potassium homeostasis during disease progression of Alzheimer's disease
Abstract figure legend Schematic diagram depicting astrocytic potassium (K+) clearance in the hippocampus of healthy brain (left) and during progression of Alzheimer's disease. Reduced conductivity through Kir channels and gap junctions in hippocampal astrocytes impair their ability to clear K+ from the extracellular milleu, which results in a ...
Evgeniia Samokhina +5 more
wiley +1 more source
Potassium channels in epithelial transport [PDF]
Epithelial cells in the kidney, gastrointestinal tract and exocrine glands are engaged in vectorial transport of salt and nutrients. In these tissues, K+ channels play an important role for the stabilization of membrane voltage and maintenance of the ...
Warth, Richard
core
Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels
Heteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express many different Kir subunits.
Konstas, A, Korbmacher, C, Tucker, S
openaire +3 more sources
The role of GαO-mediated signaling in the rostral ventrolateral medulla oblongata in cardiovascular reflexes and control of cardiac ventricular excitability. [PDF]
The heart is controlled by the sympathetic and parasympathetic limbs of the autonomic nervous system with inhibitory signaling mechanisms recruited in both limbs.
Aziz +42 more
core +2 more sources
Modulation of Kir4.2 rectification properties and pHi-sensitive run-down by association with Kir5.1
Inwardly rectifying K+ channels (Kir) comprise seven subfamilies that can be subdivided further on the basis of cytosolic pH (pHi) sensitivity, rectification strength and kinetics, and resistance to run-down. Although distinct residues within each channel subunit define these properties, heteromeric association with other Kir subunits can modulate them.
Lam, Hung D. +4 more
openaire +2 more sources
Regulation of ClC‐K/barttin by endocytosis influences distal convoluted tubule hyperplasia
Abstract figure legend ClC‐K/barttin channels mediate chloride transport in the kidney and inner ear. Mutating tyrosine 98 to alanine in barttin increases function by an unknown mechanism. In the present study, we performed experiments in oocytes and kidney cells, showing that tyrosine 98 is part of an endocytic motif.
Clara Mayayo‐Vallverdú +16 more
wiley +1 more source

