Metabolic phosphatase moonlights for proteins

Review Biochemistry & Molecular Biology

Preferential redox regulation of cysteine-based protein tyrosine phosphatases: structural and biochemical diversity

Luis Eduardo S. Netto et al.

Summary: Protein phosphorylation is an important post-translational modification involved in cell signalling. This review focuses on the biochemical and structural features of protein tyrosine phosphatases (PTPs) and their regulation by reversible oxidation. The authors discuss the oxidation products of PTPs and propose possible mechanisms for the apparent contradiction between biological and chemical redox aspects of PTPs.

FEBS JOURNAL (2022)

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Article Cell Biology

Fructose-1,6-bisphosphatase 1 functions as a protein phosphatase to dephosphorylate histone H3 and suppresses PPARα-regulated gene transcription and tumour growth

Zheng Wang et al.

Summary: Tumour cells exhibit greater metabolic plasticity than normal cells, but the mechanisms behind their selective advantages for survival and proliferation are not fully understood. This study found that glucose deprivation in normal hepatocytes induces PERK-mediated FBP1 S170 phosphorylation, leading to nuclear translocation and suppression of PPAR alpha-mediated beta-oxidation gene expression. In contrast, hepatocellular carcinoma cells exhibit O-GlcNAcylation of FBP1 S124, which inhibits FBP1 S170 phosphorylation and enhances beta-oxidation for tumour growth.

NATURE CELL BIOLOGY (2022)

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Article Oncology