The human sperm proteome 2.0: An integrated resource for studying sperm functions at the level of posttranslational modification.
The human sperm proteome 2.0: An integrated resource for studying sperm functions at the level of posttranslational modification.
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人类精子蛋白质组 2.0：用于在翻译后修饰水平上研究精子功能的综合资源。
DOI：
10.1002/pmic.201600233
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发表时间：
2016
期刊：
影响因子：
3.4
通讯作者：
Zhou Tao
中科院分区：
文献类型：
--
作者：
Wang Ying;Wan Jinyuan;Ling Xiufeng;Liu Mingxi;Zhou Tao
各种类型的PTM在精子蛋白的调节中起重要作用。然而，由于富集方法的限制，大多数大规模蛋白质组学研究仅关注单一类型的修饰。为了研究修饰精子蛋白的复杂组成，我们构建了人类精子蛋白质组2.0，该蛋白质组2.0整合了来自先前发表的蛋白质组数据集的赖氨酸乙酰化、磷酸化、N-连接糖基化和蛋白质N-末端乙酰化蛋白质。共注释了2132个蛋白质上的6069个修饰位点。功能富集分析表明，不同类型的修饰精子蛋白具有不同的功能分布。我们发现乙酰化、磷酸化和糖基化蛋白质更直接地参与精子功能。而N-末端乙酰化蛋白质和未修饰蛋白质似乎与基本细胞功能更相关。因此，在乙酰化、磷酸化和糖基化蛋白质中寻找生育相关生物标志物是有效的。我们还预测了相同蛋白质内或不同蛋白质之间的修饰串扰，这些蛋白质为理解通过多种修饰调节精子功能提供了潜在的热点目标。
Various types of PTMs play important roles in the regulation of sperm proteins. However, most large‐scale proteomic studies only focused on a single type of modification due to the limitation of enrichment methods. To investigate the complex composition of modified sperm proteins, we constructed the human sperm proteome 2.0 that integrated lysine acetylated, phosphorylated, N‐linked glycosylated, and protein N‐terminal acetylated proteins from previously published proteomic datasets. A total of 6069 modified sites on 2132 proteins were annotated. Functional enrichment analyses showed that different types of modified sperm proteins displayed different functional distributions. We found that acetylated, phosphorylated, and glycosylated proteins are more directly involved in sperm functions. While N‐termnial acetylated proteins and nonmodified proteins appear to be more associated with the basic cellular functions. Thus, it is efficient to search for fertility‐associated biomarkers in acetylated, phosphorylated, and glycosylated proteins. We also predicted modification cross‐talks within the same proteins or between different proteins that provided potential hotspot targets for understanding the regulation of sperm functions via multiple modifications.