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Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome

During brain development, synapses undergo structural rearrangements and functional changes mediated by many molecular processes including post-translational modifications by the Small Ubiquitin-like MOdifier (SUMO). To get an overview of the endogenous SUMO-modified proteins in the developing rat b...

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Autores principales: Kieffer, Félicie, Pronot, Marie, Gay, Anne-Sophie, Debayle, Delphine, Gwizdek, Carole
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9062222/
https://www.ncbi.nlm.nih.gov/pubmed/35516005
http://dx.doi.org/10.1016/j.dib.2022.108151
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author Kieffer, Félicie
Pronot, Marie
Gay, Anne-Sophie
Debayle, Delphine
Gwizdek, Carole
author_facet Kieffer, Félicie
Pronot, Marie
Gay, Anne-Sophie
Debayle, Delphine
Gwizdek, Carole
author_sort Kieffer, Félicie
collection PubMed
description During brain development, synapses undergo structural rearrangements and functional changes mediated by many molecular processes including post-translational modifications by the Small Ubiquitin-like MOdifier (SUMO). To get an overview of the endogenous SUMO-modified proteins in the developing rat brain synapses, our first aim was to characterize the synaptic proteome from rat at 14 postnatal days (PND14), a period that combines intense synaptogenesis, neurotransmission and high levels of SUMO2/3-ylation. In this purpose, we isolated the synaptosomal fraction by differential centrifugation on sucrose percoll gradient and characterized the synaptosomal proteome by nanoLC-MS/MS. Our second aim was to provide a comprehensive list of the SUMO2/3-modified protein in this compartment. We thus performed an enrichment in SUMO2/3-ylated proteins from the synaptosomal fraction by denaturing immunoprecipitation using specific anti-SUMO2/3 antibodies prior to proteomics analysis. The information presented in this article complement the publication “Proteomic Identification of an Endogenous Synaptic SUMOylome in the Developing Rat Brain” [1], by focusing on the characterization of the synaptic proteome of PND14 rat brain. Altogether, these data can inform future experiments focused on studying the functional consequences of synaptic SUMOylation regarding synapses structure and function. In addition, they can provide the basis for future mechanistic studies investigating brain pathologies involving altered SUMOylation levels.
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spelling pubmed-90622222022-05-04 Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome Kieffer, Félicie Pronot, Marie Gay, Anne-Sophie Debayle, Delphine Gwizdek, Carole Data Brief Data Article During brain development, synapses undergo structural rearrangements and functional changes mediated by many molecular processes including post-translational modifications by the Small Ubiquitin-like MOdifier (SUMO). To get an overview of the endogenous SUMO-modified proteins in the developing rat brain synapses, our first aim was to characterize the synaptic proteome from rat at 14 postnatal days (PND14), a period that combines intense synaptogenesis, neurotransmission and high levels of SUMO2/3-ylation. In this purpose, we isolated the synaptosomal fraction by differential centrifugation on sucrose percoll gradient and characterized the synaptosomal proteome by nanoLC-MS/MS. Our second aim was to provide a comprehensive list of the SUMO2/3-modified protein in this compartment. We thus performed an enrichment in SUMO2/3-ylated proteins from the synaptosomal fraction by denaturing immunoprecipitation using specific anti-SUMO2/3 antibodies prior to proteomics analysis. The information presented in this article complement the publication “Proteomic Identification of an Endogenous Synaptic SUMOylome in the Developing Rat Brain” [1], by focusing on the characterization of the synaptic proteome of PND14 rat brain. Altogether, these data can inform future experiments focused on studying the functional consequences of synaptic SUMOylation regarding synapses structure and function. In addition, they can provide the basis for future mechanistic studies investigating brain pathologies involving altered SUMOylation levels. Elsevier 2022-04-10 /pmc/articles/PMC9062222/ /pubmed/35516005 http://dx.doi.org/10.1016/j.dib.2022.108151 Text en © 2022 The Author(s). Published by Elsevier Inc. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Data Article
Kieffer, Félicie
Pronot, Marie
Gay, Anne-Sophie
Debayle, Delphine
Gwizdek, Carole
Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome
title Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome
title_full Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome
title_fullStr Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome
title_full_unstemmed Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome
title_short Proteomics datasets of developing rat brain: Synaptic proteome and SUMO2/3-ylome
title_sort proteomics datasets of developing rat brain: synaptic proteome and sumo2/3-ylome
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9062222/
https://www.ncbi.nlm.nih.gov/pubmed/35516005
http://dx.doi.org/10.1016/j.dib.2022.108151
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