Lysine crotonylation (Kcr) is a newly identified protein translational modification and is involved in major biological processes including glycolysis, but its role in colorectal cancer (CRC) is unknown. Here, we found that the Kcr of α enolase (ENO1) was significantly elevated in human CRC tissues compared with the paratumoral tissues. CREB-binding protein (CBP) functioned as a crotonyltranferase of ENO1, and SIRT2 was involved in the decrotonylation of ENO1. Using quantitative mass spectrometry for crotonylomics analysis, we further found that K420 was the main Kcr site of ENO1 and ENO1 K420 Kcr promoted the growth, migration, and invasion of CRC cells in vitro by enhancing the activity of ENO1 and regulating the expression of tumor-associated genes. Our study reveals an important mechanism by which ENO1 regulates CRC through crotonylation.

赖氨酸巴豆酰化 (Kcr) 是一种新发现的蛋白质翻译修饰，参与包括糖酵解在内的主要生物过程，但其在结直肠癌 (CRC) 中的作用尚不清楚。在这里，我们发现与瘤旁组织相比，人类 CRC 组织中的 α 烯醇化酶 (ENO1) 的 Kcr 显着升高。CREB ​​结合蛋白 (CBP) 作为 ENO1 的巴豆酰基转移酶起作用，而 SIRT2 参与 ENO1 的去巴豆酰基化。使用定量质谱进行巴豆组学分析，我们进一步发现 K420 是 ENO1 的主要 Kcr 位点，ENO1 K420 Kcr 通过增强 ENO1 的活性和调节肿瘤-相关基因。我们的研究揭示了 ENO1 通过巴豆酰化调节 CRC 的重要机制。