Kieffer Félicie, Pronot Marie, Gay Anne-Sophie, Debayle Delphine, Gwizdek Carole
Université Côte d'Azur, Centre National de la Recherche Scientifique, Institut de Pharmacologie Moléculaire et Cellulaire, France.
Data Brief. 2022 Apr 10;42:108151. doi: 10.1016/j.dib.2022.108151. eCollection 2022 Jun.
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.
在大脑发育过程中，突触会经历结构重排和功能变化，这些变化由许多分子过程介导，包括小泛素样修饰物（SUMO）的翻译后修饰。为了全面了解发育中的大鼠脑突触内源性SUMO修饰的蛋白质，我们的首要目标是表征出生后14天（PND14）大鼠的突触蛋白质组，这一时期结合了强烈的突触形成、神经传递以及高水平的SUMO2/3化。为此，我们通过在蔗糖 Percoll 梯度上进行差速离心分离突触体组分，并通过纳升液相色谱-串联质谱（nanoLC-MS/MS）对突触体蛋白质组进行表征。我们的第二个目标是提供该组分中SUMO2/3修饰蛋白质的确切清单。因此，在进行蛋白质组学分析之前，我们使用特异性抗SUMO2/3抗体通过变性免疫沉淀从突触体组分中富集SUMO2/3化蛋白质。本文所呈现的信息补充了《发育中大鼠脑内源性突触SUMO化蛋白质组的蛋白质组学鉴定》[1]这篇论文，重点关注PND14大鼠脑突触蛋白质组的表征。总之，这些数据可为未来专注于研究突触SUMO化对突触结构和功能的功能影响的实验提供参考。此外，它们还可为未来研究涉及SUMO化水平改变的脑部疾病的机制研究提供基础。
