ArticleProceedings of the National Academy of Sciences of the United States of America1996
Receptor stimulation causes slow inhibition of IRK1 inwardly rectifying K+ channels by direct protein kinase A-mediated phosphorylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 91 citations in OpenAlex.
- Beta-Adrenergic Activation of the Inward Rectifier KInternational journal of molecular sciences · 2024Article
- Tetramisole is a new IPharmacology research & perspectives · 2022Review
- Proteomic Analysis of the Functional Inward Rectifier Potassium Channel (Kir) 2.1 Reveals Several Novel Phosphorylation Sites.Biochemistry · 2021Article
- Cardiac potassium inward rectifier Kir2: Review of structure, regulation, pharmacology, and arrhythmogenesis.Heart rhythm · 2021Review
- Inhibition of cardiac potassium currents by oxidation-activated protein kinase A contributes to early afterdepolarizations in the heart.American journal of physiology. Heart and circulatory physiology · 2020Article
- Genetic Loss ofCirculation. Arrhythmia and electrophysiology · 2020Article
- Bioelectric Properties of Myogenic Progenitor Cells.Bioelectricity · 2019Review
- Boosting the signal: Endothelial inward rectifier KMicrocirculation (New York, N.Y. : 1994) · 2017Review
- Potassium currents in the heart: functional roles in repolarization, arrhythmia and therapeutics.The Journal of physiology · 2017Review
- Fluid flow facilitates inward rectifier KScientific reports · 2016Article
- Article
- Beta-adrenergic stimulation reverses the I Kr-I Ks dominant pattern during cardiac action potential.Pflugers Archiv : European journal of physiology · 2014Article
- KCNJ2 mutation causes an adrenergic-dependent rectification abnormality with calcium sensitivity and ventricular arrhythmia.Heart rhythm · 2014Article
- Autism gene variant causes hyperserotonemia, serotonin receptor hypersensitivity, social impairment and repetitive behavior.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Acute Ca(2+)-dependent desensitization of 5-HT(1A) receptors is mediated by activation of protein kinase A (PKA) in rat serotonergic neurons.Neuroscience · 2010Article
- Protein kinase A-dependent biophysical phenotype for V227F-KCNJ2 mutation in catecholaminergic polymorphic ventricular tachycardia.Circulation. Arrhythmia and electrophysiology · 2009Article
- PI3K/Akt signalling-mediated protein surface expression sensed by 14-3-3 interacting motif.The FEBS journal · 2009Article
- Mass spectrometric analysis reveals a functionally important PKA phosphorylation site in a Kir3 channel subunit.Pflugers Archiv : European journal of physiology · 2009Article
- Protein kinase C dependent inhibition of the heteromeric Kir4.1-Kir5.1 channel.Biochimica et biophysica acta · 2007Article
- Regulation of a family of inwardly rectifying potassium channels (Kir2) by the m1 muscarinic receptor and the small GTPase Rho.Pflugers Archiv : European journal of physiology · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Strongly rectifying IRK-type inwardly rectifying K+ channels are involved in the control of neuronal excitability in the mammalian brain. Whole-cell patch-clamp experiments show that cloned rat IRK1 (Kir 2.1) channels, when heterologously expressed in mammalian COS-7 cells, are inhibited following the activation of coexpressed serotonin (5-hydroxytryptamine) type 1A receptors by receptor agonists. Inhibition is mimicked by internal perfusion with GTP[gamma-S] and elevation of internal cAMP concentrations. Addition of the catalytic subunits of protein kinase A (PKA) to the internal recording solution causes complete inhibition of wild-type IRK1 channels, but not of mutant IRK1(S425N) channels in which a C-terminal PKA phosphorylation site has been removed. Our data suggest that in the nervous system serotonin may negatively control IRK1 channel activity by direct PKA-mediated phosphorylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.