Phosphoglycerate kinase 1 (PGK1) catalyzes the conversion of 1,3-bisphosphoglyceride (1,3-BPG) and ADP into 3-phosphate (3-PG) and ATP, which is a key process of glycolysis. PGK1 is considered a major regulator of various events, including one-carbon metabolism, serine biosynthesis and cell redox regulation. In the past decade, PGK1 has been found to be closely associated with various malignancies, making it a potential therapeutic target. PGK1 is involved in a series of biological processes related to tumorigenesis through post-translational modifications and various signaling pathways. PGK1 not only can participate in glucose metabolism but also acts as a protein kinase to participate in EMT, autophagy, angiogenesis, DNA replication and other processes related to tumor development. However, PGK1 also acts as a disulfide reductase to inhibit tumor by affecting angiogenesis. Exploring the structure, function and posttranslational modification of PGK1 will be helpful in further understanding the effect of metabolism on tumor progression. This manuscript reviews the role and mechanism of PGK1 in human malignancies, providing the theoretical basis for PGK1 as a possible clinical anticancer target.
Keywords: Biomarker; Cancer; Glycolysis; Phosphoglycerate kinase 1; Posttranslational modification.
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