Proteomics and phosphoproteomics datasets of a muscle-specific STIM1 loss-of-function mouse model.

STIM1 is an ER/SR transmembrane protein that interacts with ORAI1 to activate store operated Ca2+ entry (SOCE) upon ER/SR depletion of calcium. Normally highly expressed in skeletal muscle, STIM1 deficiency causes significant changes to mitochondrial ultrastructure that do not occur with loss of ORAI1 or other components of SOCE. The datasets in this article are from large-scale proteomics and phosphoproteomics experiments in an inducible mouse model of skeletal muscle-specific STIM1 knock out (KO). These data reveal statistically significant changes in the relative abundance of specific proteins and sites of protein phosphorylation in STIM1 KO gastrocnemius. Protein samples from five biological replicates of each condition (+/- STIM1) were enzymatically digested, the resulting peptides labeled with tandem mass tag (TMT) reagents, mixed, and fractionated. Phosphopeptides were enriched and a small amount of each input retained for protein abundance analysis. All phosphopeptide and input fractions were analyzed by nano LC-MS/MS on a Q Exactive Plus Orbitrap mass spectrometer, searched with Proteome Discoverer software, and processed with in-house R-scripts for data normalization and statistical analysis.STIM1是一种内质网/肌浆网（ER/SR）跨膜蛋白，可与ORAI1相互作用，在ER/SR内钙耗竭时激活钙池操纵性钙内流（store operated Ca2+ entry, SOCE）。该蛋白通常在骨骼肌中高表达，STIM1缺失会导致线粒体超微结构发生显著改变，而该改变不会因ORAI1或SOCE其他组分的缺失而出现。本文所用数据集来源于诱导型骨骼肌特异性STIM1敲除（knock out, KO）小鼠模型中的大规模蛋白质组学与磷酸化蛋白质组学实验。这些数据揭示了STIM1敲除小鼠腓肠肌中特定蛋白质及蛋白质磷酸化位点的相对丰度存在具有统计学显著性的改变。将两种实验条件（敲除/未敲除STIM1）各5份生物学重复的蛋白质样本进行酶解，所得肽段用串联质量标签（tandem mass tag, TMT）试剂标记，随后混合并进行分级分离。对磷酸化肽段进行富集，并保留每份初始样本的少量提取物用于蛋白质丰度分析。所有磷酸化肽段分级组分与初始样本分级组分均采用Q Exactive Plus Orbitrap质谱仪进行纳米液相色谱-串联质谱（nano LC-MS/MS）分析，使用Proteome Discoverer软件进行数据库检索，并通过自研R脚本完成数据归一化与统计学分析。