ArticleThe Journal of biological chemistry2011
Sialic acids attached to O-glycans modulate voltage-gated potassium channel gating.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- O-linked glycan-dependent gating of TPC2 controls lysosomal excitability and organelle remodeling.Nature communications · 2026Article
- Profiling the pancreatic cancer secretome with metabolic glycoengineering.The Journal of biological chemistry · 2026Article
- Assessment of Lectin Staining Biomarkers using a Murine Model of GNE Myopathy.microPublication biology · 2025Article
- Protein glycosylation in cardiovascular health and disease.Nature reviews. Cardiology · 2024Review
- Potassium Channels, Glucose Metabolism and Glycosylation in Cancer Cells.International journal of molecular sciences · 2023Review
- Enzyme-Digested Edible Bird's Nest (EBND) Prevents UV and Arid Environment-Induced Cellular Oxidative Stress, Cell Death and DNA Damage in Human Skin Keratinocytes and Three-Dimensional Epithelium Equivalents.Antioxidants (Basel, Switzerland) · 2023Article
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- Dendritic Excitability and Synaptic Plasticity In Vitro and In Vivo.Neuroscience · 2022Review
- Tissue specific expression of sialic acid metabolic pathway: role in GNE myopathy.Journal of muscle research and cell motility · 2021Article
- Wheat germ agglutinin-conjugated fluorescent pH sensors for visualizing proton fluxes.The Journal of general physiology · 2020Article
- Pulsed Low-Frequency Magnetic Fields Induce Tumor Membrane Disruption and Altered Cell Viability.Biophysical journal · 2020Article
- Remarkable Homeostasis of Protein Sialylation in Skeletal Muscles of Hibernating Daurian Ground Squirrels (Frontiers in physiology · 2020Article
- Reduced myocyte complex N-glycosylation causes dilated cardiomyopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Accumulation of α-2,6-sialyoglycoproteins in the Muscle Sarcoplasm Due toOpen life sciences · 2019Article
- βScientific reports · 2017Article
- Possible role of sialylation of retinal protein glycans in the regulation of electroretinogram response in mice.International journal of ophthalmology · 2017Article
- Sialic acids attached to N- and O-glycans within the Nav1.4 D1S5-S6 linker contribute to channel gating.Biochimica et biophysica acta · 2015Article
- Reduced sialylation impacts ventricular repolarization by modulating specific K+ channel isoforms distinctly.The Journal of biological chemistry · 2015Article
- Article
- Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function.Biochemical and biophysical research communications · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuronal, cardiac, and skeletal muscle action potentials are produced and conducted through the highly regulated activity of several types of voltage-gated ion channels. Voltage-gated potassium (K(v)) channels are responsible for action potential repolarization. Glycans can be attached to glycoproteins through N- and O-linkages. Previous reports described the impact of N-glycans on voltage-gated ion channel function. Here, we show that sialic acids attached through O-linkages modulate gating of K(v)2.1, K(v)4.2, and K(v)4.3. The conductance-voltage (G-V) relationships for each isoform were shifted uniquely by a depolarizing 8-16 mV under conditions of reduced sialylation. The data indicate that sialic acids modulate K(v) channel activation through apparent electrostatic mechanisms that promote channel activity. Voltage-dependent steady-state inactivation was unaffected by changes in sialylation. N-Linked sialic acids cannot be responsible for the G-V shifts because K(v)4.2 and K(v)4.3 cannot be N-glycosylated, and immunoblot analysis confirmed K(v)2.1 is not N-glycosylated. Glycosidase gel shift analysis suggested that K(v)2.1, K(v)4.2, and K(v)4.3 were O-glycosylated and sialylated. To confirm this, azide-modified sugar residues involved specifically in O-glycan and sialic acid biosynthesis were shown to incorporate into all three K(v) channel isoforms using Cu(I)-catalyzed cycloaddition chemistry. Together, the data indicate that sialic acids attached to O-glycans uniquely modulate gating of three K(v) channel isoforms that are not N-glycosylated. These data provide the first evidence that external O-glycans, with core structures distinct from N-glycans in type and number of sugar residues, can modulate K(v) channel function and thereby contribute to changes in electrical signaling that result from regulated ion channel expression and/or O-glycosylation.
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