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Dynamic regulation of eEF1A1 acetylation affects colorectal carcinogenesis

  • Hongpeng Jiang , Yu Zhang , Boya Liu , Xin Yang , Zhe Wang , Meng Han , Huiying Li EMAIL logo , Jianyuan Luo ORCID logo EMAIL logo and Hongwei Yao EMAIL logo
Published/Copyright: November 25, 2022
Biological Chemistry
From the journal Biological Chemistry Volume 404 Issue 6

Abstract

The dysregulation of the translation elongation factor families which are responsible for reprogramming of mRNA translation has been shown to contribute to tumor progression. Here, we report that the acetylation of eukaryotic Elongation Factor 1 Alpha 1 (eEF1A1/EF1A1) is required for genotoxic stress response and maintaining the malignancy of colorectal cancer (CRC) cells. The evolutionarily conserved site K439 is identified as the key acetylation site. Tissue expression analysis demonstrates that the acetylation level of eEF1A1 K439 is higher than paired normal tissues. Most importantly, hyperacetylation of eEF1A1 at K439 negatively correlates with CRC patient survival. Mechanistically, CBP and SIRT1 are the major acetyltransferase and deacetylase of eEF1A1. Hyperacetylation of eEF1A1 at K439 shows a significant tumor-promoting effect by increasing the capacity of proliferation, migration, and invasion of CRC cells. Our findings identify the altered post-translational modification at the translation machines as a critical factor in stress response and susceptibility to colorectal carcinogenesis.

Keywords: acetylation; colorectal cancer; eEF1A1; genotoxic stress; translation elongation
Corresponding authors: Huiying Li, College of Biological Sciences and Technology, Beijing Key Laboratory of Food Processing and Safety in Forest, Beijing Forestry University, Beijing 100083, P.R. China, E-mail: ; Jianyuan Luo, Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing 100191, P.R. China, E-mail: ; and Hongwei Yao, Beijing Key Laboratory of Cancer Invasion and Metastasis Research and National Clinical Research Center for Digestive Diseases; Department of General Surgery, Beijing Friendship Hospital, Capital Medical University, 95 Yong-an Road, Xi-Cheng District, Beijing 100050, P.R. China, E-mail:
Hongpeng Jiang and Yu Zhang contributed equally to this work.

Funding source: National Natural Science Foundation of China

Award Identifier / Grant number: 82203464

Funding source: Research Foundation of Beijing Friendship Hospital, Capital Medical University

Award Identifier / Grant number: yyqdkt2019-14

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: This research was funded by the Research Foundation of Beijing Friendship Hospital (No. yyqdkt2019-14) and National Natural Science Foundation of China (No. 82203464).

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Supplementary Material

The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2022-0180).

Received: 2022-05-12
Accepted: 2022-11-07
Published Online: 2022-11-25
Published in Print: 2023-05-25

© 2022 Walter de Gruyter GmbH, Berlin/Boston

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https://doi.org/10.1515/hsz-2022-0180
Keywords for this article
acetylation; colorectal cancer; eEF1A1; genotoxic stress; translation elongation

Articles in the same Issue

  1. Frontmatter
  2. Reviews
  3. Unravelling the genetic links between Parkinson’s disease and lung cancer
  4. Small-molecule metabolites in SARS-CoV-2 treatment: a comprehensive review
  5. Research Articles/Short Communications
  6. Molecular Medicine
  7. Dynamic regulation of eEF1A1 acetylation affects colorectal carcinogenesis
  8. New lipophilic organic nitrates: candidates for chronic skin disease therapy
  9. Cell Biology and Signaling
  10. Altered population activity and local tuning heterogeneity in auditory cortex of Cacna2d3-deficient mice
  11. Inhibition of miR-143-3p alleviates myocardial ischemia reperfusion injury via limiting mitochondria-mediated apoptosis
  12. Proteolysis
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