2. Academic Validation
  3. Upregulation of α enolase (ENO1) crotonylation in colorectal cancer and its promoting effect on cancer cell metastasis

Upregulation of α enolase (ENO1) crotonylation in colorectal cancer and its promoting effect on cancer cell metastasis

  • Biochem Biophys Res Commun. 2021 Nov 12;578:77-83. doi: 10.1016/j.bbrc.2021.09.027.
Jia-Yi Hou 1,  Jing Cao 2,  Li-Juan Gao 2,  Fu-Peng Zhang 3,  Jing Shen 2,  Lan Zhou 2,  Jian-Yun Shi 2,  Yan-Lin Feng 2,  Zi Yan 2,  De-Ping Wang 2,  Ji-Min Cao 4
Affiliations

Affiliations

  • 1 Key Laboratory of Cellular Physiology at Shanxi Medical University, Ministry of Education, Key Laboratory of Cellular Physiology of Shanxi Province, And the Department of Physiology, Shanxi Medical University, Taiyuan, China; Department of Clinical Laboratory, Shanxi Provincial Academy of Traditional Chinese Medicine, Taiyuan, China.
  • 2 Key Laboratory of Cellular Physiology at Shanxi Medical University, Ministry of Education, Key Laboratory of Cellular Physiology of Shanxi Province, And the Department of Physiology, Shanxi Medical University, Taiyuan, China.
  • 3 National Clinical Research Base of Traditional Chinese Medicine, Shanxi Hospital of Traditional Chinese Medicine, Taiyuan, China.
  • 4 Key Laboratory of Cellular Physiology at Shanxi Medical University, Ministry of Education, Key Laboratory of Cellular Physiology of Shanxi Province, And the Department of Physiology, Shanxi Medical University, Taiyuan, China. Electronic address: caojimin@sxmu.edu.cn.
PMID: 34547627 DOI: 10.1016/j.bbrc.2021.09.027
Abstract

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.

Keywords

Colorectal cancer; Enzyme activity; Lysine crotonylation; α enolase.

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