Glucose-sensitive acetylation of Seryl tRNA synthetase regulates lipid synthesis in breast cancer
Open accessAbstract
Abnormally enhanced de novo lipid biosynthesis has been increasingly realized to play crucial roles in the initiation and progression of varieties of cancers including breast cancer. However, the mechanisms underlying the dysregulation of lipid biosynthesis in breast cancer remain largely unknown. Here, we reported that seryl tRNA synthetase (SerRS), a key enzyme for protein biosynthesis, could translocate into the nucleus in a glucose-dependent manner to suppress key genes involved in the de novo lipid biosynthesis. In normal mammary gland epithelial cells glucose can promote the nuclear translocation of SerRS by increasing the acetylation of SerRS at lysine 323. In SerRS knock-in mice bearing acetylation-defective lysine to arginine mutation, we observed increased body weight and adipose tissue mass. In breast cancer cells the acetylation and nuclear translocation of SerRS are greatly inhibited. Overexpression of SerRS, in particularly the acetylation-mimetic lysine to glutamine mutant, dramatically inhibits the de novo lipid synthesis and hence greatly suppresses the proliferation of breast cancer cells and the growth of breast cancer xenografts in mice. We further identified that HDAC4 and HDAC5 regulated the acetylation and nuclear translocation of SerRS. Thus, we identified a SerRS-meditated inhibitory pathway in glucose-induced lipid biosynthesis, which is dysregulated in breast cancer.
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In the normal breast, glucose controls lipid biosynthesis by regulating nuclear import of SerRS via an acetylation switch.
“In the normal breast, glucose controls lipid biosynthesis by regulating nuclear import of SerRS via an acetylation switch.”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Zhao et al., 2021
HDAC4 and HDAC5 are the deacetylases that control the acetylation and nuclear translocation of SerRS, thus boosting lipid metabolism and cell growth.
“HDAC4 and HDAC5 are the deacetylases that control the acetylation and nuclear translocation of SerRS, thus boosting lipid metabolism and cell growth (Zhao et al., 2021).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Zhao et al., 2021
HDAC4 is associated with de novo lipid biosynthesis.
“HDAC4 is also associated with de novo lipid biosynthesis.”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Zhao et al., 2021
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- Authors
- Zhao, J., Bai, H., Li, X., Yan, J., Zou, G., Wang, L., Li, X., Liu, Z., Xiang, R., Yang, X.-L., & Shi, Y.
- Affiliations
- Nankai University (CN)
- Scripps Research Institute (US)
- Corresponding author
- Shi, Yi
- ORCID
- Venue
- Signal Transduction and Targeted Therapy
- Published
- 2021-08-16
- Volume
- 6
- Issue
- 1
- Pages
- 303-303
- ISSN
- 2059-3635 (ISSN-L)
- PMC
- PMC8368063
- OpenAlex
- W3195596607
- Cited by
- 27
- References
- 45
- Citations by year
- 2026: 7 · 2025: 4 · 2024: 6 · 2023: 4 · 2022: 6
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Signal Transduction and Targeted Therapy (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (81772974, 81972882)
- Bilateral Inter-Governmental S&T Cooperation Project from Ministry of Science and Technology of China
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- seryl-tRNA synthetase, surface-enhanced resonance Raman scattering, lysine acetylation, nuclear translocation, glucose metabolism, breast cancer, HDAC4, HDAC5, histone deacetylase, adipose tissue mass, tumor cell proliferation
- MeSH terms
- Acetylation, Adipose Tissue, Amino Acid Sequence, Animals, Breast Neoplasms, Female, Glucose, Histone Deacetylases, Humans, Lipids, Serine-tRNA Ligase, Substrate Specificity, Gene Expression Regulation, Neoplastic, Active Transport, Cell Nucleus, Mice, Gene Knock-In Techniques, Heterografts
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