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Quantitative subcellular proteomics analyses of TNF-alpha activated mouse macrophages highlight the selective degradation of mitochondria by mitophagy

机译:TNF-α活化小鼠巨噬细胞的定量亚细胞蛋白质组学分析突出了MITOCHAD的选择性降解

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We identified 1586, 1495 and 3305 protein in phagosome, endosome and membrane fractions using our large-scale quantitative proteomics workflow. 409 proteins were differentially abundant upon TNF-alpha stimulation. Gene Ontology analysis revealed the enrichment of mitochondria proteins as downregulated proteins upon TNF-alpha stimulation. Protein interaction analyses identified clusters of autophagy-related proteins as well as Traf6, an important regulator of endosome functions. The induction of mitophagy in response to TNF-alpha was confirmed using functional validation.
机译:我们使用我们的大规模定量蛋白质组学的工作流程确定了吞噬体组,内体和膜级分中的1586,1495和3305蛋白。在TNF-α刺激时,409个蛋白质差异丰富。基因本体分析显示,在TNF-α刺激时,线粒体蛋白质的富集为下调蛋白。蛋白质相互作用分析鉴定了相关蛋白质的簇以及TRAF6,是内体功能的重要调节因子。使用功能验证确认了响应TNF-α的响应TNF-α的诱导。

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