Protein kinase function of pyruvate kinase M2 and cancer

Cancer Cell International

Shangwu Chen¹  Xun Chen²  Dongsheng Yu² 

[1] Department of Biochemistry, Guangdong Key Laboratory of Pharmaceutical Functional Genes, MOE Key Laboratory of Gene Function and Regulation, State Key Laboratory for Biocontrol, School of Life Sciences, Sun Yat-sen University, 510275, Guangzhou, People’s Republic of China;Department of Oral and Maxillofacial Surgery, Guangdong Provincial Key Laboratory of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, 56 Lingyuan West Road, 510055, Guangzhou, People’s Republic of China;

关键词: Pyruvate kinase M2;    Protein kinase;    Glycolytic pathway;    Non-metabolic function;    Tumorigenesis;   

DOI  :  10.1186/s12935-020-01612-1

来源: Springer

【 摘 要 】

Pyruvate kinase is a terminal enzyme in the glycolytic pathway, where it catalyzes the conversion of phosphoenolpyruvate to pyruvate and production of ATP via substrate level phosphorylation. PKM2 is one of four isoforms of pyruvate kinase and is widely expressed in many types of tumors and associated with tumorigenesis. In addition to pyruvate kinase activity involving the metabolic pathway, increasing evidence demonstrates that PKM2 exerts a non-metabolic function in cancers. PKM2 has been shown to be translocated into nucleus, where it serves as a protein kinase to phosphorylate various protein targets and contribute to multiple physiopathological processes. We discuss the nuclear localization of PKM2, its protein kinase function and association with cancers, and regulation of PKM2 activity.

【 授权许可】

CC BY