Proteomics

Dataset Information

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

ABSTRACT: Synaptic transmission is an ultra-fast process that aims at transducing a signal from one neuron to another neuron or cell by the release of neurotransmitters. This process requires rapid response which can be transmitted through fast molecular switches such as post-translational modifications of proteins. We aimed at investigating the potential importance in dynamic modulation of sialic acids on N-linked glycoproteins that are essential for the synaptic transmission process. For this, we characterize site-specific alteration in sialylated N-linked glycosylation in the active zone of rat nerve terminals (synaptosomes) after depolarization by using quantitative sialiomics.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Brain

SUBMITTER: Inga Matthies  

LAB HEAD: Martin R. Larsen

PROVIDER: PXD016230 | Pride | 2020-06-12

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
Exp1_SDS-insoluble_formerlysialylatedN-linkedglycopeptides.pdResult Other
Exp1_SDS-soluble_formerlysialylatedN-linkedglycopeptides.pdResult Other
Exp2_SDS-insoluble_formerlysialylatedN-linkedglycopeptides.pdResult Other
Exp2_SDS-insoluble_non-modified.pdResult Other
Exp2_SDS-insoluble_non-modified_secondsearchwithreducedglycoproteindatabase.pdResult Other
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Publications

Depolarization-dependent Induction of Site-specific Changes in Sialylation on <i>N-</i>linked Glycoproteins in Rat Nerve Terminals.

Boll Inga I   Jensen Pia P   Schwämmle Veit V   Larsen Martin R MR  

Molecular & cellular proteomics : MCP 20200609 9

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 that sialylation of <i>N</i>-linked glycosylation is a novel potential modulator of neurotransmitter release mechanisms by investigating depolarization-dependent changes of formerly sialylated <i>N</i>-linked glycopeptides. We suggest that neg  ...[more]

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