乳酰化作为一种​​新型的翻译后修饰，对于研究蛋白质在生理和病理过程中的功能和调控，以及深入了解包括肿瘤在内的多种疾病的发生和发展至关重要。然而，很少有研究检查整个生物体的蛋白质乳酰化。因此，我们研究了秀丽隐杆线虫中整体蛋白的乳酰化以获得体内乳酰化。使用基于 MS 的平台，我们在 487 种蛋白质中鉴定出了 1836 个 I 类（定位概率 > 0.75）乳酰化位点。生物信息学分析表明，乳酰化蛋白主要定位于细胞质，参与三羧酸循环（TCA循环）等代谢途径。然后，我们评估了不同生物体中乳酰化的保守性。总共有 41 种线虫蛋白被乳酰化，并且与人类和大鼠的乳酰化蛋白同源。此外，H4K80 上的乳酰化在三个物种中是保守的。首次在秀丽隐杆线虫中鉴定出另外 238 个乳酰化蛋白。这项研究建立了第一个线虫乳酰化数据库，并为研究乳酰化的作用提供了基础。© 2023 作者。蛋白质组学由 Wiley-VCH GmbH 出版。

Lactylation, as a novel posttranslational modification, is essential for studying the functions and regulation of proteins in physiological and pathological processes, as well as for gaining in-depth knowledge on the occurrence and development of many diseases, including tumors. However, few studies have examined the protein lactylation of one whole organism. Thus, we studied the lactylation of global proteins in Caenorhabditis elegans to obtain an in vivo lactylome. Using an MS-based platform, we identified 1836 Class I (localization probabilities > 0.75) lactylated sites in 487 proteins. Bioinformatics analysis showed that lactylated proteins were mainly located in the cytoplasm and involved in the tricarboxylic acid cycle (TCA cycle) and other metabolic pathways. Then, we evaluated the conservation of lactylation in different organisms. In total, 41 C. elegans proteins were lactylated and homologous to lactylated proteins in humans and rats. Moreover, lactylation on H4K80 was conserved in three species. An additional 238 lactylated proteins were identified in C. elegans for the first time. This study establishes the first lactylome database in C. elegans and provides a basis for studying the role of lactylation.© 2023 The Authors. Proteomics published by Wiley-VCH GmbH.