Lactylation: Linking the Warburg effect to DNA damage repair

Peng Sun; Leina Ma; Zhimin Lu

doi:10.1016/j.cmet.2024.06.015

Lactylation: Linking the Warburg effect to DNA damage repair

Cell Metab. 2024 Aug 6;36(8):1637-1639. doi: 10.1016/j.cmet.2024.06.015.

Authors

Peng Sun¹, Leina Ma¹, Zhimin Lu²

Affiliations

¹ Department of Hepatobiliary and Pancreatic Surgery, Department of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
² Zhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital and Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, China; Cancer Center, Zhejiang University, Hangzhou, Zhejiang 310029, China; Institute of Fundamental and Transdisciplinary Research, Zhejiang University, Hangzhou, Zhejiang 310029, China. Electronic address: zhiminlu@zju.edu.cn.

PMID: 39111282
DOI: 10.1016/j.cmet.2024.06.015

Abstract

In this issue of Cell Metabolism, Li et al. report that the highly expressed aldehyde dehydrogenase 1 family member A3 interacts with pyruvate kinase M2 (PKM2) in glioblastoma cells. Consequently, PKM2 tetramerization and activation promote lactate production, leading to the lactylation and nuclear translocation of XRCC1 for DNA damage repair and therapeutic resistance.

MeSH terms

Aldehyde Dehydrogenase / genetics
Aldehyde Dehydrogenase / metabolism
Carrier Proteins / metabolism
DNA Damage*
DNA Repair*
DNA-Binding Proteins / metabolism
Glioblastoma / genetics
Glioblastoma / metabolism
Glioblastoma / pathology
Humans
Membrane Proteins / metabolism
Thyroid Hormone-Binding Proteins
Thyroid Hormones / metabolism
Warburg Effect, Oncologic
X-ray Repair Cross Complementing Protein 1 / metabolism

Substances

DNA-Binding Proteins
X-ray Repair Cross Complementing Protein 1
Thyroid Hormone-Binding Proteins
XRCC1 protein, human
Thyroid Hormones
Membrane Proteins
Carrier Proteins
Aldehyde Dehydrogenase