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Inwardly rectifying K(+) (Kir) channels allow K(+) to move more easily into rather than out of the cell. They have diverse physiological functions depending on their type and their location. There are seven Kir channel subfamilies that can be classified into four functional groups: classical Kir channels (Kir2. x) are constitutively active, G protein-gated Kir channels (Kir3. x) are regulated by G protein-coupled receptors, ATP-sensitive K(+) channels (Kir6.
 Some inward rectifiers, termed "weak inward rectifiers", carry measurable outward K+ currents at voltages positive to the K+ reversal potential (corresponding to, but larger than, the small currents above the 0 nA line in figure 1). They, along with the "leak" channels, establish the resting membrane potential of the cell. Other inwardly rectifying channels.
The question is how these might act to reinforce normal heart rhythm or act as substrates for cardiac arrhythmia. We have specific interests in a range of potassium channels and heterotrimeric G-protein signalling in the heart and blood vessels. Technically we are using unique strains of genetically modified mice and we combine this with murine phenotyping capabilities including single-cell electrophysiology and imaging of cardiac myocytes (ventricular, atrial and SA nodal), telemetry and electrophysiology studies. In addition, we also have an established track record in molecular and cellular studies in these areas and are still performing such work. I have several very distinctive research strands being pursued in my laboratory with a focus on ATP-sensitive K+ channels, G-protein gated inwardly rectifying K+ channels.
Another family of ion channels, the inwardly rectifying K+ channels, has no voltage-sensor domain but has a pore-forming domain with much sequence identity and ion selectivity identical to that of voltage-gated K+ channels. Such evolutionary diversification suggests an early origin of modular ion-selective pore domains for tetrameric channels and of voltage-sensor domains that could be appended to them.
The GABA(B) receptor is a G-protein coupled receptor (GPCR) that associates with a subset of G-proteins (pertussis toxin sensitive Gi/o family), that in turn regulate specific ion channels and trigger cAMP cascades. In this review, we describe the relationships between the GABA(B) receptor, its effectors and associated proteins that mediate GABA(B) receptor function within the brain. We discuss a unique feature of the GABA(B) receptor, the requirement for heterodimerization to produce functional receptors, as well as an increasing body of evidence that suggests GABA(B) receptors comprise a macromolecular signaling heterocomplex, critical for efficient targeting and function of the receptors. Within this complex, GABA(B) receptors associate specifically with Gi/o G-proteins that regulate voltage-gated Ca(2+) (Ca(V)) channels, G-protein activated inwardly rectifying K(+) (GIRK) channels.
Sakura H, Bond C, Warren-Perry M, Horsley S, Kearney L, Tucker S, Adelman J, Turner R, Ashcroft FM (August 1995). "Characterization and variation of a human inwardly-rectifying-K-channel gene (KCNJ6): a putative ATP-sensitive K-channel subunit". FEBS Lett 367 (2): 193–7. doi:10. 1016/0014-5793(95)00498-X. PMID 7796919.
VU591 is a Potassium Inwardly-Rectifying Channel (KCNJ1 or ROMK) specific inhibitor (IC50 = 240 nM) that is closely related to VU590. Unlike VU590, VU591 does not inhibit Kir7. 1. The compound has a modest effect on Kir6. 2/SUR1, causing 17% inhibition at 10 uM.