ArticlePloS one2011
Importance of glycosylation on function of a potassium channel in neuroblastoma cells.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Potassium Channels, Glucose Metabolism and Glycosylation in Cancer Cells.International journal of molecular sciences · 2023Review
- Kv3-Expressing Cells Present More Elaborate N-Glycans with Changes in Cytoskeletal Proteins, Neurite Structure and Cell Migration.COJ biomedical science & research · 2023Article
- Compromised N-Glycosylation Processing of Kv3.1b Correlates with Perturbed Motor Neuron Structure and Locomotor Activity.Biology · 2021Article
- Review
- Article
- Article
- The glycosylation of the extracellular loop of β2 subunits diversifies functional phenotypes of BK Channels.Channels (Austin, Tex.) · 2017Article
- Membrane Distribution and Activity of a Neuronal Voltage-Gated K+ Channel is Modified by Replacement of Complex Type N-Glycans with Hybrid Type.Journal of glycobiology · 2017Article
- Glycoproteins Enrichment and LC-MS/MS Glycoproteomics in Central Nervous System Applications.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Predominant Expression of Hybrid N-Glycans Has Distinct Cellular Roles Relative to Complex and Oligomannose N-Glycans.International journal of molecular sciences · 2016Article
- Sialic acids attached to N- and O-glycans within the Nav1.4 D1S5-S6 linker contribute to channel gating.Biochimica et biophysica acta · 2015Article
- A recurrent de novo mutation in KCNC1 causes progressive myoclonus epilepsy.Nature genetics · 2015Article
- Complex N-Glycans Influence the Spatial Arrangement of Voltage Gated Potassium Channels in Membranes of Neuronal-Derived Cells.PloS one · 2015Article
- Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function.Biochemical and biophysical research communications · 2014Review
- N-glycosylation-dependent control of functional expression of background potassium channels K2P3.1 and K2P9.1.The Journal of biological chemistry · 2013Article
- Glycan structures contain information for the spatial arrangement of glycoproteins in the plasma membrane.PloS one · 2013Article
- Mapping N-linked glycosylation sites in the secretome and whole cells of Aspergillus niger using hydrazide chemistry and mass spectrometry.Journal of proteome research · 2012Article
- Mining the virgin land of neurotoxicology: a novel paradigm of neurotoxic peptides action on glycosylated voltage-gated sodium channels.Journal of toxicology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Kv3.1 glycoprotein, a voltage-gated potassium channel, is expressed throughout the central nervous system. The role of N-glycans attached to the Kv3.1 glycoprotein on conducting and non-conducting functions of the Kv3.1 channel are quite limiting. Glycosylated (wild type), partially glycosylated (N220Q and N229Q), and unglycosylated (N220Q/N229Q) Kv3.1 proteins were expressed and characterized in a cultured neuronal-derived cell model, B35 neuroblastoma cells. Western blots, whole cell current recordings, and wound healing assays were employed to provide evidence that the conducting and non-conducting properties of the Kv3.1 channel were modified by N-glycans of the Kv3.1 glycoprotein. Electrophoretic migration of the various Kv3.1 proteins treated with PNGase F and neuraminidase verified that the glycosylation sites were occupied and that the N-glycans could be sialylated, respectively. The unglycosylated channel favored a different whole cell current pattern than the glycoform. Further the outward ionic currents of the unglycosylated channel had slower activation and deactivation rates than those of the glycosylated Kv3.1 channel. These kinetic parameters of the partially glycosylated Kv3.1 channels were also slowed. B35 cells expressing glycosylated Kv3.1 protein migrated faster than those expressing partially glycosylated and much faster than those expressing the unglycosylated Kv3.1 protein. These results have demonstrated that N-glycans of the Kv3.1 glycoprotein enhance outward ionic current kinetics, and neuronal migration. It is speculated that physiological changes which lead to a reduction in N-glycan attachment to proteins will alter the functions of the Kv3.1 channel.
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