Álvarez-Salamero Candelas, Castillo-González Raquel, Navarro María N
Departamento de Medicina, Universidad Autónoma de Madrid, Madrid, Spain.
Instituto de Investigación Sanitaria del Hospital Universitario de La Princesa, Madrid, Spain.
Front Immunol. 2017 Aug 9;8:938. doi: 10.3389/fimmu.2017.00938. eCollection 2017.
Phosphorylation is the most abundant post-translational modification, regulating several aspects of protein and cell function. Quantitative phosphoproteomics approaches have expanded the scope of phosphorylation analysis enabling the quantification of changes in thousands of phosphorylation sites simultaneously in two or more conditions. These approaches offer a global view of the impact of cellular perturbations such as extracellular stimuli or gene ablation in intracellular signaling networks. Such great potential also brings on a new challenge: to identify, among the thousands of phosphorylations found in global phosphoproteomics studies, the small subset of site-specific phosphorylations expected to be functionally relevant. This review focus on updating and integrating findings on T lymphocyte signaling generated using global phosphoproteomics approaches, drawing attention on the biological relevance of the obtained data.
磷酸化是最丰富的翻译后修饰,调节蛋白质和细胞功能的多个方面。定量磷酸蛋白质组学方法扩展了磷酸化分析的范围,能够在两种或更多条件下同时对数千个磷酸化位点的变化进行定量。这些方法提供了细胞扰动(如细胞外刺激或基因敲除)对细胞内信号网络影响的全局视图。如此巨大的潜力也带来了一个新的挑战:在全局磷酸蛋白质组学研究中发现的数千种磷酸化中,识别出预期具有功能相关性的一小部分位点特异性磷酸化。本综述着重于更新和整合使用全局磷酸蛋白质组学方法产生的关于T淋巴细胞信号传导的研究结果,提请关注所获数据的生物学相关性。