ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2008
Interdomain cytoplasmic interactions govern the intracellular trafficking, gating, and modulation of the Kv2.1 channel.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Pentameric assembly of the Kv2.1 tetramerization domain.Acta crystallographica. Section D, Structural biology · 2022Article
- Controlling ion channel function with renewable recombinant antibodies.The Journal of physiology · 2022Review
- Regulation of neuronal excitation-transcription coupling by Kv2.1-induced clustering of somatic L-type CaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- The S6 gate in regulatory Kv6 subunits restricts heteromeric KThe Journal of general physiology · 2018Article
- Cleavage of potassium channel Kv2.1 by BACE2 reduces neuronal apoptosis.Molecular psychiatry · 2018Article
- The Segregated Expression of Voltage-Gated Potassium and Sodium Channels in Neuronal Membranes: Functional Implications and Regulatory Mechanisms.Frontiers in cellular neuroscience · 2017Article
- Convergent phosphomodulation of the major neuronal dendritic potassium channel Kv4.2 by pituitary adenylate cyclase-activating polypeptide.Neuropharmacology · 2016Article
- Two di-leucine motifs regulate trafficking and function of mouse ASIC2a.Molecular brain · 2016Article
- Cell Cycle-dependent Changes in Localization and Phosphorylation of the Plasma Membrane Kv2.1 K+ Channel Impact Endoplasmic Reticulum Membrane Contact Sites in COS-1 Cells.The Journal of biological chemistry · 2015Article
- Distinct Cell- and Layer-Specific Expression Patterns and Independent Regulation of Kv2 Channel Subtypes in Cortical Pyramidal Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Target of HIV-1 Envelope Glycoprotein gp120-Induced Hippocampal Neuron Damage: Role of Voltage-Gated K(+) Channel Kv2.1.Viral immunology · 2015Article
- Kv1.3 contains an alternative C-terminal ER exit motif and is recruited into COPII vesicles by Sec24a.BMC biochemistry · 2015Article
- Article
- Domain structure and conformational changes in rat KV2.1 ion channel.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2014Article
- Ionic mechanisms in pancreatic β cell signaling.Cellular and molecular life sciences : CMLS · 2014Review
- Syntaxin-binding domain of Kv2.1 is essential for the expression of apoptotic K+ currents.The Journal of physiology · 2014Article
- Leptin modulates the intrinsic excitability of AgRP/NPY neurons in the arcuate nucleus of the hypothalamus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Specific sorting and post-Golgi trafficking of dendritic potassium channels in living neurons.The Journal of biological chemistry · 2014Article
- Voltage-gated potassium channels at the crossroads of neuronal function, ischemic tolerance, and neurodegeneration.Translational stroke research · 2014Review
- The subfamily-specific interaction between Kv2.1 and Kv6.4 subunits is determined by interactions between the N- and C-termini.PloS one · 2014Article
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3 authors.
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Abstract
Voltage-gated potassium (Kv) channels comprise four transmembrane alpha subunits, often associated with cytoplasmic beta subunits that impact channel expression and function. Here, we show that cell surface expression, voltage-dependent activation gating, and phosphorylation-dependent modulation of Kv2.1 are regulated by cytoplasmic N/C interaction within the alpha subunit. Kv2.1 surface expression is greatly reduced by C-terminal truncation. Tailless Kv2.1 channels exhibit altered voltage-dependent gating properties and lack the bulk of the phosphorylation-dependent modulation of channel gating. Remarkably, the soluble C terminus of Kv2.1 associates with tailless channels and rescues their expression, function, and phosphorylation-dependent modulation. Soluble N and C termini of Kv2.1 can also interact directly. We also show that the N/C-terminal interaction in Kv2.1 is governed by a 34 aa motif in the juxtamembrane cytoplasmic C terminus, and a 17 aa motif located in the N terminus at a position equivalent to the beta subunit binding site in other Kv channels. Deletion of either motif disrupts N/C-terminal interaction and surface expression, function, and phosphorylation-dependent modulation of Kv2.1 channels. These findings provide novel insights into intrinsic mechanisms for the regulation of Kv2.1 trafficking, gating, and phosphorylation-dependent modulation through cytoplasmic N/C-terminal interaction, which resembles alpha/beta subunit interaction in other Kv channels.
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