ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000
Neuronal inwardly rectifying K(+) channels differentially couple to PDZ proteins of the PSD-95/SAP90 family.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 119 citations in OpenAlex.
- Roles of neuroligins in central nervous system development: focus on glial neuroligins and neuron neuroligins.Journal of translational medicine · 2022Review
- The Potassium Channel Odyssey: Mechanisms of Traffic and Membrane Arrangement.International journal of molecular sciences · 2019Review
- Domain insertion permissibility-guided engineering of allostery in ion channels.Nature communications · 2019Article
- Lipopolysaccharides increase Kir2.1 expression in lung endothelial cells.International journal of clinical and experimental pathology · 2018Article
- Protein crowding and lipid complexity influence the nanoscale dynamic organization of ion channels in cell membranes.Scientific reports · 2017Article
- GIRK2 splice variants and neuronal G protein-gated KScientific reports · 2017Article
- Boosting the signal: Endothelial inward rectifier KMicrocirculation (New York, N.Y. : 1994) · 2017Review
- Expression of Kir4.1 and Kir5.1 inwardly rectifying potassium channels in oligodendrocytes, the myelinating cells of the CNS.Brain structure & function · 2017Article
- Article
- Channel properties of Nax expressed in neurons.PloS one · 2015Article
- Protein kinase A-phosphorylated KV1 channels in PSD95 signaling complex contribute to the resting membrane potential and diameter of cerebral arteries.Circulation research · 2014Article
- Firing modes of dopamine neurons drive bidirectional GIRK channel plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Up-regulation of the inwardly rectifying K⁺ channel Kir2.1 (KCNJ2) by protein kinase B (PKB/Akt) and PIKfyve.The Journal of membrane biology · 2013Article
- Dynamic reciprocity of sodium and potassium channel expression in a macromolecular complex controls cardiac excitability and arrhythmia.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Developmental regulation of G protein-gated inwardly-rectifying K+ (GIRK/Kir3) channel subunits in the brain.The European journal of neuroscience · 2011Article
- Novel etiopathophysiological aspects of thyrotoxic periodic paralysis.Nature reviews. Endocrinology · 2011Review
- Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Kir2.6 regulates the surface expression of Kir2.x inward rectifier potassium channels.The Journal of biological chemistry · 2011Article
- Regulation of cardiac inward rectifier potassium current (I(K1)) by synapse-associated protein-97.The Journal of biological chemistry · 2010Article
- Emerging roles for G protein-gated inwardly rectifying potassium (GIRK) channels in health and disease.Nature reviews. Neuroscience · 2010Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several signaling proteins clustered at the postsynaptic density specialization in neurons harbor a conserved C-terminal PDZ domain recognition sequence (X-S/T-X-V/I) that mediates binding to members of the PSD-95/SAP90 protein family. This motif is also present in the C termini of some inwardly rectifying K(+) (Kir) channels. Constitutively active Kir2 channels as well as G protein-gated Kir3 channels, which are fundamental for neuronal excitability, were analyzed as candidates for binding to PSD-95/SAP90 family members. Therefore C termini of Kir2.1(+), Kir2.3(+), Kir2.4(-), Kir3.1(-), Kir3.2(+), Kir3.3(+) and Kir3.4(-) subunits (+, motif present; -, motif absent) were used as baits in the yeast two-hybrid assay to screen for in vivo interaction with PDZ domains 1-3 of PSD-95/SAP90. In contrast to Kir2.1 and Kir2.3, all Kir3 fragments failed to bind PSD-95 in this assay, which was supported by the lack of coimmunoprecipitation and colocalization of the entire proteins in mammalian cells. A detailed analysis of interaction domains demonstrated that the C-terminal motif in Kir3 channels is insufficient for binding PDZ domains. Kir2.1 and Kir2.3 subunits on the other hand coprecipitate with PSD-95. When coexpressed in a bicistronic internal ribosome entry site expression vector in HEK-293 cells macroscopic and elementary current analysis revealed that PSD-95 suppressed the activity of Kir2.3 channels by >50%. This inhibitory action of PSD-95, which predominantly affects the single-channel conductance, is likely attributable to a molecular association with additional internal interaction sites in the Kir2.3 protein.
Indexed as
Identifiers
10627592PMC6774109W2122326942What OpenQuestion holds
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.