PreprintCited by 32Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisCellular transport and secretion

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Synaptic transmission induces site-specific changes in sialylation on N -linked glycoproteins in rat nerve terminals

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Boll, Inga, Jensen, Pia, Schwämmle, Veit, Larsen, Martin R.·2020·Molecular & Cellular Proteomics

Preprint — published as 10.1074/mcp.ra119.001896 · Paper page

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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Metadata

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
openRxiv
Published
2020-04-06
Volume
19
Issue
9
Pages
1418-1435
ISSN
1535-9476 (ISSN-L)
OpenAlex
W3033064440
Cited by
32
References
1
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
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
  • Natur og Univers, Det Frie Forskningsråd
  • VILLUM Center for Bioanalytical Sciences
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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