Depolarization-dependent Induction of Site-specific Changes in Sialylation on N-linked Glycoproteins in Rat Nerve Terminals
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Abstract
Abstract Synaptic transmission leading to release of neurotransmitters in the nervous system is a fast and highly dynamic process. Previously, protein interaction and phosphorylation have been thought to be the main regulators of synaptic transmission. Here we show a novel potential modulator of synaptic transmission, sialylation of N -linked glycosylation. The negatively charged sialic acids can be modulated, similarly to phosphorylation, by the action of sialyltransferases and sialidases thereby changing local structure and function of membrane glycoproteins. We characterized site-specific alteration in sialylation on N- linked glycoproteins in isolated rat nerve terminals after brief depolarization using quantitative sialiomics. We identified 1965 formerly sialylated N- linked glycosites in synaptic proteins and found that the abundances of 430 glycosites changed after five seconds depolarization. We observed changes on essential synaptic proteins such as synaptic vesicle proteins, ion channels and transporters, neurotransmitter receptors and cell adhesion molecules. This study is to our knowledge the first to describe ultra-fast site-specific modulation of the sialiome after brief stimulation of a biological system.
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- Authors
- Boll, I., Jensen, P., Schwämmle, V., & Larsen, M. R.
- Affiliations
- University of Southern Denmark (DK)
- Corresponding author
- Larsen, Martin R.
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2020-09
- Volume
- 19
- Issue
- 9
- Pages
- 1418-1435
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC8143646
- OpenAlex
- W3033064440
- Cited by
- 32
- References
- 6
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 2 · 2023: 7 · 2022: 3 · 2021: 6 · 2020: 1
- FWCI
- 1.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- University of Southern Denmark Research Portal (University of Southern Denmark) (submittedVersion, cc-by)
- Funders
- Danish Natural Science Research Council (6108-00621B)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- sialylation, N-linked glycoproteins, depolarization, presynaptic terminals, synaptic transmission, neurotransmitter release, sialyltransferase, neuraminidase, synaptic vesicle proteins, ion channels, neurotransmitter receptors, adhesion molecules, membrane glycoproteins
- MeSH terms
- Animals, Chlorates, Chromatography, Liquid, Glycosides, Glycosylation, Male, Membrane Glycoproteins, Peripheral Nerves, Sialic Acids, Synapses, Synaptic Membranes, Signal Transduction, Receptors, N-Methyl-D-Aspartate, Rats, Sprague-Dawley, Neurotransmitter Agents, Proteome, Proteomics, Rats, Tandem Mass Spectrometry
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