The aging process is affected by many environmental factors including temperature. Protein phosphorylation is an important post-translational modification that regulates various life activities and also plays an important role in the aging process. Caenorhabditis elegans (C. elegans) is a classic model organism for aging research. In order to explore the role of protein phosphorylation modification in the aging process at different temperatures, we carried out phosphoproteomic analysis on C. elegans samples on the 1st, 5th, and 10th days of the adult stage under the culture conditions of 20 °C (normal temperature) and 25 °C (high temperature). We adopted a label-free quantitative analysis method based on DIA to systematically compare the phosphoproteomic differences among different samples. A total of 9,145 high-confidence phosphorylated peptides were identified, corresponding to 3,317 phosphorylated proteins. After screening, 6,624 phosphorylated peptides were finally quantified, among which 1,093 significantly changed phosphorylated peptides were from 858 phosphorylated proteins, containing 1,426 phosphorylation sites. Through further bioinformatics analysis, the phosphorylation change rules in the aging process were revealed.
衰老过程受到包括温度在内的众多环境因素的影响。蛋白质磷酸化是重要的翻译后修饰,调控多种生命活动,在衰老过程中也起着重要作用。秀丽隐杆线虫(Caenorhabditis elegans,C.elegans)是经典的衰老研究的模式生物。为了探究蛋白质磷酸化修饰在不同温度下衰老过程中的作用,我们对20℃(常温)和25℃(高温)培养条件下成年时期第1天、第5天、第10天的秀丽隐杆线虫样品进行了磷酸化组学分析工作。我们采用基于DIA的非标定量分析方法,系统地比较了不同样品间的磷酸化组学差异。共9 145条高可信度的磷酸化肽段被鉴定到,对应3 317个磷酸化蛋白质。经过筛选,最终6 624条磷酸化肽段被定量到,其中有1 093条显著变化的磷酸化肽段,来自于858个磷酸化蛋白质,包含1 426个磷酸化位点,通过进一步的生物信息学分析,揭示了衰老过程中的磷酸化变化规律。