ArticleThe Journal of biological chemistry2013
N-glycosylation-dependent control of functional expression of background potassium channels K2P3.1 and K2P9.1.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 22 citations in OpenAlex.
- The cryo-EM structure and physical basis for anesthetic inhibition of the THIK1 K2P channel.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Research progress of two-pore potassium channel in myocardial ischemia-reperfusion injury.Frontiers in physiology · 2024Review
- Potassium Channels, Glucose Metabolism and Glycosylation in Cancer Cells.International journal of molecular sciences · 2023Review
- Evaluation of the Ion Channel Assembly in a Eukaryotic Cell-Free System Focusing on Two-Pore Domain Potassium Channels KInternational journal of molecular sciences · 2023Article
- Thalamocortical circuits drive remifentanil-induced postoperative hyperalgesia.The Journal of clinical investigation · 2022Article
- Article
- N-glycosylation-dependent regulation of hKMolecular biology of the cell · 2019Article
- The Potassium Channel Odyssey: Mechanisms of Traffic and Membrane Arrangement.International journal of molecular sciences · 2019Review
- Article
- Cooperative roles of glucose and asparagine-linked glycosylation in T-type calcium channel expression.Pflugers Archiv : European journal of physiology · 2016Article
- Developmental conditioning of endothelium-derived hyperpolarizing factor-mediated vasorelaxation.Journal of hypertension · 2016Article
- TASK-1 Regulates Apoptosis and Proliferation in a Subset of Non-Small Cell Lung Cancers.PloS one · 2016Article
- Endocytosis as a mode to regulate functional expression of two-pore domain potassium (K₂p) channels.Pflugers Archiv : European journal of physiology · 2015Review
- Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex.The Biochemical journal · 2013Article
- Article
- Acid sensitive background potassium channels K2P3.1 and K2P9.1 undergo rapid dynamin-dependent endocytosis.Channels (Austin, Tex.)Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Two-pore domain potassium (K(2P)) channels play fundamental roles in cellular processes by enabling a constitutive leak of potassium from cells in which they are expressed, thus influencing cellular membrane potential and activity. Hence, regulation of these channels is of critical importance to cellular function. A key regulatory mechanism of K(2P) channels is the control of their cell surface expression. Membrane protein delivery to and retrieval from the cell surface is controlled by their passage through the secretory and endocytic pathways, and post-translational modifications regulate their progression through these pathways. All but one of the K(2P) channels possess consensus N-linked glycosylation sites, and here we demonstrate that the conserved putative N-glycosylation site in K(2P)3.1 and K(2P)9.1 is a glycan acceptor site. Patch clamp analysis revealed that disruption of channel glycosylation reduced K(2P)3.1 current, and flow cytometry was instrumental in attributing this to a decreased number of channels on the cell surface. Similar findings were observed when cells were cultured in reduced glucose concentrations. Disruption of N-linked glycosylation has less of an effect on K(2P)9.1, with a small reduction in number of channels on the surface observed, but no functional implications detected. Because nonglycosylated channels appear to pass through the secretory pathway in a manner comparable with glycosylated channels, the evidence presented here suggests that the decreased number of nonglycosylated K(2P)3.1 channels on the cell surface may be due to their decreased stability.
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