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Journal articles on the topic 'Kir3'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Hibino, Hiroshi, Atsushi Inanobe, Kazuharu Furutani, Shingo Murakami, Ian Findlay, and Yoshihisa Kurachi. "Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles." Physiological Reviews 90, no. 1 (2010): 291–366. http://dx.doi.org/10.1152/physrev.00021.2009.

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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.x) are tightly linked to cellular metabolism, and K+transport channels (Kir1.x, Kir4.x, Kir5.x, and Kir7.x). Inward rectification results from pore block by intracellular substances such as Mg2+and polyamines. Kir channel activity can be modulated by ions, phospholipids, and binding proteins. The basic building block of a Kir channel is made up of two transmembrane helices with cytoplasmic NH2and COOH termini and an extracellular loop which folds back to form the pore-lining ion selectivity filter. In vivo, functional Kir channels are composed of four such subunits which are either homo- or heterotetramers. Gene targeting and genetic analysis have linked Kir channel dysfunction to diverse pathologies. The crystal structure of different Kir channels is opening the way to understanding the structure-function relationships of this simple but diverse ion channel family.

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2

Walsh, Kenneth B. "Screening Technologies for Inward Rectifier Potassium Channels: Discovery of New Blockers and Activators." SLAS DISCOVERY: Advancing the Science of Drug Discovery 25, no. 5 (2020): 420–33. http://dx.doi.org/10.1177/2472555220905558.

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K+ channels play a critical role in maintaining the normal electrical activity of excitable cells by setting the cell resting membrane potential and by determining the shape and duration of the action potential. In nonexcitable cells, K+ channels establish electrochemical gradients necessary for maintaining salt and volume homeostasis of body fluids. Inward rectifier K+ (Kir) channels typically conduct larger inward currents than outward currents, resulting in an inwardly rectifying current versus voltage relationship. This property of inward rectification results from the voltage-dependent block of the channels by intracellular polyvalent cations and makes these channels uniquely designed for maintaining the resting potential near the K+ equilibrium potential (EK). The Kir family of channels consist of seven subfamilies of channels (Kir1.x through Kir7.x) that include the classic inward rectifier (Kir2.x) channel, the G-protein-gated inward rectifier K+ (GIRK) (Kir3.x), and the adenosine triphosphate (ATP)-sensitive (KATP) (Kir 6.x) channels as well as the renal Kir1.1 (ROMK), Kir4.1, and Kir7.1 channels. These channels not only function to regulate electrical/electrolyte transport activity, but also serve as effector molecules for G-protein-coupled receptors (GPCRs) and as molecular sensors for cell metabolism. Of significance, Kir channels represent promising pharmacological targets for treating a number of clinical conditions, including cardiac arrhythmias, anxiety, chronic pain, and hypertension. This review provides a brief background on the structure, function, and pharmacology of Kir channels and then focuses on describing and evaluating current high-throughput screening (HTS) technologies, such as membrane potential-sensitive fluorescent dye assays, ion flux measurements, and automated patch clamp systems used for Kir channel drug discovery.

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3

Xie, Lai-Hua, Scott A. John, Bernard Ribalet, and James N. Weiss. "Long Polyamines Act as Cofactors in PIP2 Activation of Inward Rectifier Potassium (Kir2.1) Channels." Journal of General Physiology 126, no. 6 (2005): 541–49. http://dx.doi.org/10.1085/jgp.200509380.

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Phosphatidylinosital-4,5-bisphosphate (PIP2) acts as an essential factor regulating the activity of all Kir channels. In most Kir members, the dependence on PIP2 is modulated by other factors, such as protein kinases (in Kir1), Gβγ (in Kir3), and the sulfonylurea receptor (in Kir6). So far, however, no regulator has been identified in Kir2 channels. Here we show that polyamines, which cause inward rectification by selectively blocking outward current, also regulate the interaction of PIP2 with Kir2.1 channels to maintain channel availability. Using spermine and diamines as polyamine analogs, we demonstrate that both spontaneous and PIP2 antibody–induced rundown of Kir2.1 channels in excised inside-out patches was markedly slowed by long polyamines; in contrast, polyamines with shorter chain length were ineffective. In K188Q mutant channels, which have a low PIP2 affinity, application PIP2 (10 μM) was unable to activate channel activity in the absence of polyamines, but markedly activated channels in the presence of long diamines. Using neomycin as a measure of PIP2 affinity, we found that long polyamines were capable of strengthening either the wild type or K188Q channels' interaction with PIP2. The negatively charged D172 residue inside the transmembrane pore region was critical for the shift of channel–PIP2 binding affinity by long polyamines. Sustained pore block by polyamines was neither sufficient nor necessary for this effect. We conclude that long polyamines serve a dual role as both blockers and coactivators (with PIP2) of Kir2.1 channels.

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4

Weaver, C. David, and Jerod S. Denton. "Next-generation inward rectifier potassium channel modulators: discovery and molecular pharmacology." American Journal of Physiology-Cell Physiology 320, no. 6 (2021): C1125—C1140. http://dx.doi.org/10.1152/ajpcell.00548.2020.

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Inward rectifying potassium (Kir) channels play important roles in both excitable and nonexcitable cells of various organ systems and could represent valuable new drug targets for cardiovascular, metabolic, immune, and neurological diseases. In nonexcitable epithelial cells of the kidney tubule, for example, Kir1.1 ( KCNJ1) and Kir4.1 ( KCNJ10) are linked to sodium reabsorption in the thick ascending limb of Henle’s loop and distal convoluted tubule, respectively, and have been explored as novel-mechanism diuretic targets for managing hypertension and edema. G protein-coupled Kir channels (Kir3) channels expressed in the central nervous system are critical effectors of numerous signal transduction pathways underlying analgesia, addiction, and respiratory-depressive effects of opioids. The historical dearth of pharmacological tool compounds for exploring the therapeutic potential of Kir channels has led to a molecular target-based approach using high-throughput screen (HTS) of small-molecule libraries and medicinal chemistry to develop “next-generation” Kir channel modulators that are both potent and specific for their targets. In this article, we review recent efforts focused specifically on discovery and improvement of target-selective molecular probes. The reader is introduced to fluorescence-based thallium flux assays that have enabled much of this work and then provided with an overview of progress made toward developing modulators of Kir1.1 (VU590, VU591), Kir2.x (ML133), Kir3.X (ML297, GAT1508, GiGA1, VU059331), Kir4.1 (VU0134992), and Kir7.1 (ML418). We discuss what is known about the small molecules’ molecular mechanisms of action, in vitro and in vivo pharmacology, and then close with our view of what critical work remains to be done.

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5

Troncoso Brindeiro, Carmen M., Rachel W. Fallet, Pascale H. Lane, and Pamela K. Carmines. "Potassium channel contributions to afferent arteriolar tone in normal and diabetic rat kidney." American Journal of Physiology-Renal Physiology 295, no. 1 (2008): F171—F178. http://dx.doi.org/10.1152/ajprenal.00563.2007.

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We previously reported an enhanced tonic dilator impact of ATP-sensitive K+ channels in afferent arterioles of rats with streptozotocin (STZ)-induced diabetes. The present study explored the hypothesis that other types of K+ channel also contribute to afferent arteriolar dilation in STZ rats. The in vitro blood-perfused juxtamedullary nephron technique was utilized to quantify afferent arteriolar lumen diameter responses to K+ channel blockers: 0.1–3.0 mM 4-aminopyridine (4-AP; KV channels), 10–100 μM barium (KIR channels), 1–100 nM tertiapin-Q (TPQ; Kir1.1 and Kir3.x subfamilies of KIR channels), 100 nM apamin (SKCa channels), and 1 mM tetraethylammonium (TEA; BKCa channels). In kidneys from normal rats, 4-AP, TEA, and Ba2+ reduced afferent diameter by 23 ± 3, 8 ± 4, and 18 ± 2%, respectively, at the highest concentrations employed. Neither TPQ nor apamin significantly altered afferent diameter. In arterioles from STZ rats, a constrictor response to TPQ (22 ± 4% decrease in diameter) emerged, and the response to Ba2+ was exaggerated (28 ± 5% decrease in diameter). Responses to the other K+ channel blockers were similar to those observed in normal rats. Moreover, exposure to either TPQ or Ba2+ reversed the afferent arteriolar dilation characteristic of STZ rats. Acute surgical papillectomy did not alter the response to TPQ in arterioles from normal or STZ rats. We conclude that 1) KV, KIR, and BKCa channels tonically influence normal afferent arteriolar tone, 2) KIR channels (including Kir1.1 and/or Kir3.x) contribute to the afferent arteriolar dilation during diabetes, and 3) the dilator impact of Kir1.1/Kir3.x channels during diabetes is independent of solute delivery to the macula densa.

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6

Cha, Tae-Joon, Joachim R. Ehrlich, Denis Chartier, Xiao-Yan Qi, Ling Xiao, and Stanley Nattel. "Kir3-Based Inward Rectifier Potassium Current." Circulation 113, no. 14 (2006): 1730–37. http://dx.doi.org/10.1161/circulationaha.105.561738.

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7

Le, Robert Q., Prathima Anandi, Xin Tian, et al. "Comparison of Donor KIR Genotype, Recipient CMV Reactivation and Pretransplant MRD in Predicting Relapse after Ex Vivo T-Deplete Allohsct." Blood 126, no. 23 (2015): 3212. http://dx.doi.org/10.1182/blood.v126.23.3212.3212.

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Abstract INTRODUCTION: Relapse is the most important cause of post-transplant mortality. The interaction between killer immunoglobulin-like receptors (KIRs) of donor natural killer (NK) cells and human leukocyte antigen (HLA)-class I molecules on recipient target cells may influence the outcome of allogeneic hematopoietic stem cell transplantation (HCT) by modulating NK cell alloreactivity. In addition to modulation by KIRs, NK cells also respond to CMV reactivation post-HCT to promote maturation and functional competence that could enhance their antileukemic effect. Since NK cells are postulated to play a prominent role in the setting of ex vivo T cell depleted HCT, we studied the relative contributions of KIR-mediated alloresponse and early CMV reactivation, in addition to measurable residual disease (MRD) status, on clinical outcomes. METHODS: A cohort of 109 consecutive patients who received myeloablative, HLA-identical sibling allogeneic peripheral blood HCT for hematological malignancies was studied at a single institution. All patients received a myeloablative preparative regimen (fludarabine 125 mg/m2, cyclophosphamide 120mg/kg, total body irradiation 400-1200 cGy based on age) followed by the infusion of a CD34+ selected graft from an HLA-identical sibling. Three models of donor KIRs were evaluated: a) KIR2DS1 positive (Venstrom, et al. NEJM 2012) seen in 41% of donors, b) "KIR3" - all 3 KIRs 2DL5A, 2DS1, and 3DS1 (Stringaris, et al. BBMT 2010) seen in 34% or, c) any KIR B genotype defining loci (KIR2DL5, 2DS1, 2DS2, 2DS3, 2DS5, or 3DS1) seen in 68%. CMV reactivation (65%) was described as a time-dependent covariate as well as dichotomized into early (< Day 60) vs other. Baseline multigene array MRD status was determined by RT-PCR (Goswami, et al. BMT 2015) and found to be positive in 6/21 (29%) of AML patients. Cox proportional hazards models were used. The cumulative incidence of relapse (CIR) was estimated and compared by the Gray's method to account for competing risks. RESULTS: Median recipient age was 43 years and median HCT-CI score was 3 (range 2 - 4). 40% of the cohort had AML, 26% ALL, 19% MDS, 10% NHL/CLL and 5% CML. At a median follow up of ~ 5 years, cumulative incidence of relapse was 35.4%, overall survival (OS) was 48.3% (95% CI 39.2-59.5), and NRM was 26.5%. CMV reactivation was not significantly associated with CIR as a time-dependent covariate (HR 1.4, P =0.35) or as a dichotomized covariate (HR 1.7, P =0. 16). Donor KIR2DS1 (HR 1.8, P = 0.07), KIR3 positivity (HR 1.9, P =0.06), and any haplotype B (HR 1.5, P =0.25) were not significantly associated with CIR. In the multivariate models adjusted for age at HCT, disease risk and CMV reactivation. However, MRD status in AML subjects was highly predictive of future relapse (MRD+ CIR was 83% vs MRD- CIR 21%, HR 7.5, p = 0.0015)(Figure 1). CONCLUSIONS: Pretransplant MRD (confined to AML subjects) strongly predicted future AML relapse in our models, and there was no significant association found with early CMV reactivation or with donor KIRs. Figure 1. Cumulative Incidence of Relapse by MRD Status. Figure 1. Cumulative Incidence of Relapse by MRD Status. Disclosures No relevant conflicts of interest to declare.

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8

Keselman, Inna, Miguel Fribourg, Dan P. Felsenfeld, and Diomedes E. Logothetis. "Mechanism of PLC-Mediated Kir3 Current Inhibition." Channels 1, no. 2 (2007): 113–23. http://dx.doi.org/10.4161/chan.4321.

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9

Zylbergold, Peter, and Terence E. Hébert. "Kir3 channel signalling complexes in cardiac arrhythmias." Drug Discovery Today: Disease Models 9, no. 3 (2012): e97-e102. http://dx.doi.org/10.1016/j.ddmod.2012.02.009.

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10

Bukiya, Anna N., and Avia Rosenhouse-Dantsker. "Modulation of Neuronal Kir3 Channels by Cholesterol." Biophysical Journal 110, no. 3 (2016): 608a. http://dx.doi.org/10.1016/j.bpj.2015.11.3245.

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11

Yang, Hua-Qian, Wilnelly Martinez-Ortiz, JongIn Hwang, Xuexin Fan, Timothy J. Cardozo, and William A. Coetzee. "Palmitoylation of the KATP channel Kir6.2 subunit promotes channel opening by regulating PIP2 sensitivity." Proceedings of the National Academy of Sciences 117, no. 19 (2020): 10593–602. http://dx.doi.org/10.1073/pnas.1918088117.

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A physiological role for long-chain acyl-CoA esters to activate ATP-sensitive K+ (KATP) channels is well established. Circulating palmitate is transported into cells and converted to palmitoyl-CoA, which is a substrate for palmitoylation. We found that palmitoyl-CoA, but not palmitic acid, activated the channel when applied acutely. We have altered the palmitoylation state by preincubating cells with micromolar concentrations of palmitic acid or by inhibiting protein thioesterases. With acyl-biotin exchange assays we found that Kir6.2, but not sulfonylurea receptor (SUR)1 or SUR2, was palmitoylated. These interventions increased the KATP channel mean patch current, increased the open time, and decreased the apparent sensitivity to ATP without affecting surface expression. Similar data were obtained in transfected cells, rat insulin-secreting INS-1 cells, and isolated cardiac myocytes. Kir6.2ΔC36, expressed without SUR, was also positively regulated by palmitoylation. Mutagenesis of Kir6.2 Cys166 prevented these effects. Clinical variants in KCNJ11 that affect Cys166 had a similar gain-of-function phenotype, but was more pronounced. Molecular modeling studies suggested that palmitoyl-C166 and selected large hydrophobic mutations make direct hydrophobic contact with Kir6.2-bound PIP2. Patch-clamp studies confirmed that palmitoylation of Kir6.2 at Cys166 enhanced the PIP2 sensitivity of the channel. Physiological relevance is suggested since palmitoylation blunted the regulation of KATP channels by α1-adrenoreceptor stimulation. The Cys166 residue is conserved in some other Kir family members (Kir6.1 and Kir3, but not Kir2), which are also subject to regulated palmitoylation, suggesting a general mechanism to control the open state of certain Kir channels.

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12

Rajalingam, Raja, Mei Hong, Erin J. Adams, Benny P. Shum, Lisbeth A. Guethlein, and Peter Parham. "Short KIR Haplotypes in Pygmy Chimpanzee (Bonobo) Resemble the Conserved Framework of Diverse Human KIR Haplotypes." Journal of Experimental Medicine 193, no. 1 (2001): 135–46. http://dx.doi.org/10.1084/jem.193.1.135.

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Some pygmy chimpanzees (also called Bonobos) give much simpler patterns of hybridization on Southern blotting with killer cell immunoglobulin-like receptor (KIR) cDNA probes than do either humans or common chimpanzees. Characterization of KIRs from pygmy chimpanzees having simple and complex banding patterns identified nine different KIRs, representing seven genes. Five of these genes have orthologs in the common chimpanzee, and three of them (KIRCI, KIR2DL4, and KIR2DL5) also have human orthologs. The remaining two genes are KIR3D paralogous to the human and common chimpanzee major histocompatibility complex A– and/or -B–specific KIRs. Within a pygmy chimpanzee family, KIR haplotypes were defined. Simple patterns on Southern blot were due to inheritance of “short” KIR haplotypes containing only three KIR genes, KIRCI, KIR2DL4, and KIR3D, each of which represents one of the three major KIR lineages. These three genes in pygmy chimpanzees or their corresponding genes in humans and common chimpanzees form the conserved “framework” common to all KIR haplotypes in these species and upon which haplotypic diversity is built. The fecundity and health of individual pygmy chimpanzees who are homozygotes for short KIR haplotypes attest to the viability of short KIR haplotypes, indicating that they can provide minimal, essential KIRs for the natural killer and T cells of the hominoid immune system.

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13

Ha, Junghoon, Yu Xu, Takeharu Kawano, et al. "Hydrogen sulfide inhibits Kir2 and Kir3 channels by decreasing sensitivity to the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2)." Journal of Biological Chemistry 293, no. 10 (2018): 3546–61. http://dx.doi.org/10.1074/jbc.ra117.001679.

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14

Inanobe, Atsushi, Yoshiyuki Horio, Akikazu Fujita, Hiroshi Hibino, Yukiko Yoshimoto, and Yoshihisa Kurachi. "Immunolocalization of GIRKx/Kir3.x subunits in mouse testis." Japanese Journal of Pharmacology 76 (1998): 234. http://dx.doi.org/10.1016/s0021-5198(19)41047-0.

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15

Nelson, Cole S., Jennifer L. Marino, and Charles N. Allen. "Melatonin receptors activate heteromeric G-protein coupled Kir3 channels." NeuroReport 7, no. 3 (1996): 717–20. http://dx.doi.org/10.1097/00001756-199602290-00009.

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16

Pravetoni, M., and K. Wickman. "Behavioral characterization of mice lacking GIRK/Kir3 channel subunits." Genes, Brain and Behavior 7, no. 5 (2008): 523–31. http://dx.doi.org/10.1111/j.1601-183x.2008.00388.x.

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17

Nassirpour, Rounak, and Paul A. Slesinger. "Subunit-Specific Regulation of Kir3 Channels by Sorting nexin 27." Channels 1, no. 5 (2007): 331–33. http://dx.doi.org/10.4161/chan.5191.

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18

Styer, Amanda M., Uyenlinh L. Mirshahi, Chuan Wang та ін. "G Protein βγ Gating Confers Volatile Anesthetic Inhibition to Kir3 Channels". Journal of Biological Chemistry 285, № 53 (2010): 41290–99. http://dx.doi.org/10.1074/jbc.m110.178541.

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19

Kurokawa, Tatsuki, Shigeki Kiyonaka, Eiji Nakata, et al. "DNA Origami Scaffolds as Templates for Functional Tetrameric Kir3 K+ Channels." Angewandte Chemie International Edition 57, no. 10 (2018): 2586–91. http://dx.doi.org/10.1002/anie.201709982.

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20

Kurokawa, Tatsuki, Shigeki Kiyonaka, Eiji Nakata, et al. "DNA Origami Scaffolds as Templates for Functional Tetrameric Kir3 K+ Channels." Angewandte Chemie 130, no. 10 (2018): 2616–21. http://dx.doi.org/10.1002/ange.201709982.

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21

Morgan, Andrew D., Marilyn E. Carroll, Annemarie K. Loth, Markus Stoffel, and Kevin Wickman. "Decreased Cocaine Self-Administration in Kir3 Potassium Channel Subunit Knockout Mice." Neuropsychopharmacology 28, no. 5 (2002): 932–38. http://dx.doi.org/10.1038/sj.npp.1300100.

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22

Robitaille, Mélanie, Nitya Ramakrishnan, Alessandra Baragli, and Terence E. Hébert. "Intracellular trafficking and assembly of specific Kir3 channel/G protein complexes." Cellular Signalling 21, no. 4 (2009): 488–501. http://dx.doi.org/10.1016/j.cellsig.2008.11.011.

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23

Nagi, Karim, Iness Charfi, and Graciela Pineyro. "Kir3 channels undergo arrestin-dependant internalization following delta opioid receptor activation." Cellular and Molecular Life Sciences 72, no. 18 (2015): 3543–57. http://dx.doi.org/10.1007/s00018-015-1899-x.

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24

Kollert, Sina, Frank Döring, Ulrich Gergs, and Erhard Wischmeyer. "Chloroform is a potent activator of cardiac and neuronal Kir3 channels." Naunyn-Schmiedeberg's Archives of Pharmacology 393, no. 4 (2019): 573–80. http://dx.doi.org/10.1007/s00210-019-01751-x.

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25

Bradley, Karri K., William J. Hatton, Helen S. Mason, et al. "Kir3.1/3.2 encodes an I KACh-like current in gastrointestinal myocytes." American Journal of Physiology-Gastrointestinal and Liver Physiology 278, no. 2 (2000): G289—G296. http://dx.doi.org/10.1152/ajpgi.2000.278.2.g289.

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Expression of the Kir3 channel subfamily in gastrointestinal (GI) myocytes was investigated. Members of this K+ channel subfamily encode G protein-gated inwardly rectifying K+ channels ( I KACh) in other tissues, including the heart and brain. In the GI tract, I KACh could act as a negative feedback mechanism to temper the muscarinic response mediated primarily through activation of nonselective cation currents and inhibition of delayed-rectifier conductance. Kir3 channel subfamily isoforms expressed in GI myocytes were determined by performing RT-PCR on RNA isolated from canine colon, ileum, duodenum, and jejunum circular myocytes. Qualitative PCR demonstrated the presence of Kir3.1 and Kir3.2 transcripts in all smooth muscle cell preparations examined. Transcripts for Kir3.3 and Kir3.4 were not detected in the same preparations. Semiquantitative PCR showed similar transcriptional levels of Kir3.1 and Kir3.2 relative to β-actin expression in the various GI preparations. Full-length cDNAs for Kir3.1 and Kir3.2 were cloned from murine colonic smooth muscle RNA and coexpressed in Xenopus oocytes with human muscarinic type 2 receptor. Superfusion of oocytes with ACh (10 μM) reversibly activated a Ba2+-sensitive and inwardly rectifying K+current. Immunohistochemistry using Kir3.1- and Kir3.2-specific antibodies demonstrated channel expression in circular and longitudinal smooth muscle cells. We conclude that an I KAChcurrent is expressed in GI myocytes encoded by Kir3.1/3.2 heterotetramers.

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26

Zylbergold, Peter, Rory Sleno, and Terence E. Hébert. "A novel, radiolabel-free pulse chase strategy to study Kir3 channel ontogeny." Journal of Receptors and Signal Transduction 33, no. 3 (2013): 144–52. http://dx.doi.org/10.3109/10799893.2013.764898.

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27

Cruz, H. G., F. Berton, M. Sollini, et al. "Absence and Rescue of Morphine Withdrawal in GIRK/Kir3 Knock-out Mice." Journal of Neuroscience 28, no. 15 (2008): 4069–77. http://dx.doi.org/10.1523/jneurosci.0267-08.2008.

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28

Zhao, Qi, Takeharu Kawano, Hiroko Nakata, Yasuko Nakajima, Shigehiro Nakajima та Tohru Kozasa. "Interaction of G Protein β Subunit with Inward Rectifier K+ Channel Kir3". Molecular Pharmacology 64, № 5 (2003): 1085–91. http://dx.doi.org/10.1124/mol.64.5.1085.

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29

Adney, S. K., J. Ha, X. Y. Meng, T. Kawano, and D. E. Logothetis. "A Critical Gating Switch at a Modulatory Site in Neuronal Kir3 Channels." Journal of Neuroscience 35, no. 42 (2015): 14397–405. http://dx.doi.org/10.1523/jneurosci.1415-15.2015.

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30

Kawano, Takeharu, Peng Zhao, Christina V. Floreani, Yasuko Nakajima, Tohru Kozasa та Shigehiro Nakajima. "Interaction of Gαq and Kir3, G Protein-Coupled Inwardly Rectifying Potassium Channels". Molecular Pharmacology 71, № 4 (2007): 1179–84. http://dx.doi.org/10.1124/mol.106.032508.

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31

Slesinger, Paul A. "Insights into Gating of GIRK (KIR3) Channels through G Protein-Independent Pathways." Biophysical Journal 114, no. 3 (2018): 35a. http://dx.doi.org/10.1016/j.bpj.2017.11.248.

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32

Nimitvilai, Sudarat, Marcelo F. Lopez, Patrick J. Mulholland, and John J. Woodward. "Ethanol Dependence Abolishes Monoamine and GIRK (Kir3) Channel Inhibition of Orbitofrontal Cortex Excitability." Neuropsychopharmacology 42, no. 9 (2017): 1800–1812. http://dx.doi.org/10.1038/npp.2017.22.

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33

Schoots, Oscar, Julie M. Wilson, Nathalie Ethier, Eve Bigras, Terence E. Hebert, and Hubert H. M. Van Tol. "Co-expression of Human Kir3 Subunits Can Yield Channels with Different Functional Properties." Cellular Signalling 11, no. 12 (1999): 871–83. http://dx.doi.org/10.1016/s0898-6568(99)00059-5.

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34

Moldavan, Mykhaylo G., Robert P. Irwin, and Charles N. Allen. "Presynaptic GABAB Receptors Regulate Retinohypothalamic Tract Synaptic Transmission by Inhibiting Voltage-Gated Ca2+ Channels." Journal of Neurophysiology 95, no. 6 (2006): 3727–41. http://dx.doi.org/10.1152/jn.00909.2005.

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Presynaptic GABAB receptor activation inhibits glutamate release from retinohypothalamic tract (RHT) terminals in the suprachiasmatic nucleus (SCN). Voltage-clamp whole cell recordings from rat SCN neurons and optical recordings of Ca2+-sensitive fluorescent probes within RHT terminals were used to examine GABAB-receptor modulation of RHT transmission. Baclofen inhibited evoked excitatory postsynaptic currents (EPSCs) in a concentration-dependent manner equally during the day and night. Blockers of N-, P/Q-, T-, and R-type voltage-dependent Ca2+ channels, but not L-type, reduced the EPSC amplitude by 66, 36, 32, and 18% of control, respectively. Joint application of multiple Ca2+ channel blockers inhibited the EPSCs less than that predicted, consistent with a model in which multiple Ca2+ channels overlap in the regulation of transmitter release. Presynaptic inhibition of EPSCs by baclofen was occluded by ω-conotoxin GVIA (≤72%), mibefradil (≤52%), and ω-agatoxin TK (≤15%), but not by SNX-482 or nimodipine. Baclofen reduced both evoked presynaptic Ca2+ influx and resting Ca2+ concentration in RHT terminals. Tertiapin did not alter the evoked EPSC and baclofen-induced inhibition, indicating that baclofen does not inhibit glutamate release by activation of Kir3 channels. Neither Ba2+ nor high extracellular K+ modified the baclofen-induced inhibition. 4-Aminopyridine (4-AP) significantly increased the EPSC amplitude and the charge transfer, and dramatically reduced the baclofen effect. These data indicate that baclofen inhibits glutamate release from RHT terminals by blocking N-, T-, and P/Q-type Ca2+ channels, and possibly by activation of 4-AP–sensitive K+ channels, but not by inhibition of R- and L-type Ca2+ channels or by Kir3 channel activation.

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35

Ippolito, Danielle L., Paul A. Temkin, Sherri L. Rogalski та Charles Chavkin. "N-terminal Tyrosine Residues within the Potassium Channel Kir3 Modulate GTPase Activity of Gαi". Journal of Biological Chemistry 277, № 36 (2002): 32692–96. http://dx.doi.org/10.1074/jbc.m204407200.

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Koike-Tani, Maki, John M. Collins, Takeharu Kawano, et al. "Signal transduction pathway for the substance P-induced inhibition of rat Kir3 (GIRK) channel." Journal of Physiology 564, no. 2 (2005): 489–500. http://dx.doi.org/10.1113/jphysiol.2004.079285.

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37

Zylbergold, Peter, Nitya Ramakrishnan, and Terry Hébert. "The role of G proteins in assembly and function of Kir3 inwardly rectifying potassium channels." Channels 4, no. 5 (2010): 411–21. http://dx.doi.org/10.4161/chan.4.5.13327.

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38

Clayton, Cecilea C., Mei Xu та Charles Chavkin. "Tyrosine Phosphorylation of Kir3 following κ-Opioid Receptor Activation of p38 MAPK Causes Heterologous Desensitization". Journal of Biological Chemistry 284, № 46 (2009): 31872–81. http://dx.doi.org/10.1074/jbc.m109.053793.

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39

Zhang, Zhe, Avia Rosenhouse-Dantsker, Qiongyao Tang, Sergei Noskov, and Diomedes E. Logothetis. "The Na+-Activated Potassium Channel Slack Shares a Similar Na+ Coordination Site with Kir3 Channels." Biophysical Journal 98, no. 3 (2010): 533a—534a. http://dx.doi.org/10.1016/j.bpj.2009.12.2895.

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40

Rusinova, Radda, Yu-Ming Albert Shen, Georgia Dolios, et al. "Mass spectrometric analysis reveals a functionally important PKA phosphorylation site in a Kir3 channel subunit." Pflügers Archiv - European Journal of Physiology 458, no. 2 (2009): 303–14. http://dx.doi.org/10.1007/s00424-008-0628-9.

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41

Fowler, Catherine E., Prafulla Aryal, Ka Fai Suen, and Paul A. Slesinger. "Evidence for association of GABABreceptors with Kir3 channels and regulators of G protein signalling (RGS4) proteins." Journal of Physiology 580, no. 1 (2007): 51–65. http://dx.doi.org/10.1113/jphysiol.2006.123216.

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42

Bingen, Brian O., Zeinab Neshati, Saïd F. A. Askar, et al. "Atrium-Specific Kir3.x Determines Inducibility, Dynamics, and Termination of Fibrillation by Regulating Restitution-Driven Alternans." Circulation 128, no. 25 (2013): 2732–44. http://dx.doi.org/10.1161/circulationaha.113.005019.

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43

Fernández-Alacid, Laura, Masahiko Watanabe, Elek Molnár, Kevin Wickman, and Rafael Luján. "Developmental regulation of G protein-gated inwardly-rectifying K+ (GIRK/Kir3) channel subunits in the brain." European Journal of Neuroscience 34, no. 11 (2011): 1724–36. http://dx.doi.org/10.1111/j.1460-9568.2011.07886.x.

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44

Rogalski, Sherri L., and Charles Chavkin. "Eicosanoids Inhibit the G-protein-gated Inwardly Rectifying Potassium Channel (Kir3) at the Na+/PIP2Gating Site." Journal of Biological Chemistry 276, no. 18 (2001): 14855–60. http://dx.doi.org/10.1074/jbc.m010097200.

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45

Andersson, Sandra, Cyril Fauriat, Jenny-Ann Malmberg, Hans-Gustaf Ljunggren, and Karl-Johan Malmberg. "KIR acquisition probabilities are independent of self-HLA class I ligands and increase with cellular KIR expression." Blood 114, no. 1 (2009): 95–104. http://dx.doi.org/10.1182/blood-2008-10-184549.

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Abstract Inhibitory killer cell immunoglobulin-like receptors (KIRs) preserve tolerance to self and shape the functional response of human natural killer (NK) cells. Here, we have evaluated the influence of selection processes in the formation of inhibitory KIR repertoires in a cohort of 44 donors homozygous for the group A KIR haplotype. Coexpression of multiple KIRs was more frequent than expected by the product rule that describes random association of independent events. In line with this observation, the probability of KIR acquisition increased with the cellular expression of KIRs. Three types of KIR repertoires were distinguished that differed in frequencies of KIR- and NKG2A-positive cells but showed no dependency on the number of self-HLA class I ligands. Furthermore, the distribution of self- and nonself-KIRs at the cell surface reflected a random combination of receptors rather than a selection process conferred by cognate HLA class I molecules. Finally, NKG2A was found to buffer overall functional responses in KIR repertoires characterized by low-KIR expression frequencies. The results provide new insights into the formation of inhibitory KIR repertoires on human NK cells and support a model in which variegated KIR repertoires are generated through sequential and random acquisition of KIRs in the absence of selection.

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46

Bertrand, Sandrine, Dominique Nouel, France Morin, Fr�d�ric Nagy, and Jean-Claude Lacaille. "Gabapentin actions on Kir3 currents and N-type Ca2+ channels via GABAB receptors in hippocampal pyramidal cells." Synapse 50, no. 2 (2003): 95–109. http://dx.doi.org/10.1002/syn.10247.

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47

Johnston, April, Chris J. McBain, and André Fisahn. "5‐Hydroxytryptamine 1A receptor‐activation hyperpolarizes pyramidal cells and suppresses hippocampal gamma oscillations via Kir3 channel activation." Journal of Physiology 592, no. 19 (2014): 4187–99. http://dx.doi.org/10.1113/jphysiol.2014.279083.

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48

Eulitz, Dirk, Harald Prüss, Christian Derst, and Rüdiger W. Veh. "Heterogeneous Distribution of Kir3 Potassium Channel Proteins Within Dopaminergic Neurons in the Mesencephalon of the Rat Brain." Cellular and Molecular Neurobiology 27, no. 3 (2007): 285–302. http://dx.doi.org/10.1007/s10571-006-9118-9.

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49

Lei, Q., M. B. Jones, E. M. Talley, et al. "Activation and inhibition of G protein-coupled inwardly rectifying potassium (Kir3) channels by G protein beta gamma subunits." Proceedings of the National Academy of Sciences 97, no. 17 (2000): 9771–76. http://dx.doi.org/10.1073/pnas.97.17.9771.

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Rusinova, Radda, Tooraj Mirshahi та Diomedes E. Logothetis. "Specificity of Gβγ Signaling to Kir3 Channels Depends on the Helical Domain of Pertussis Toxin-sensitive Gα Subunits". Journal of Biological Chemistry 282, № 47 (2007): 34019–30. http://dx.doi.org/10.1074/jbc.m704928200.

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