Prolyl 3-hydroxylase OGFOD1 (OGFOD1)

Prolyl 3-hydroxylase OGFOD1 is a conserved, iron and 2-oxoglutarate-dependent enzyme that catalyzes the post-translational hydroxylation of Pro62 in the small ribosomal subunit protein S23 (RPS23/uS12). This modification regulates the accuracy and efficiency of translation termination, and impacts cellular proliferation, stress granule formation, and autophagy. OGFOD1 is part of the broad family of 2OG-dependent oxygenases, sharing structural similarity to hypoxia-inducible factor prolyl hydroxylases; its activity is sensitive to iron chelators and oxygenase inhibitors. Loss or inhibition of OGFOD1 results in decreased RPS23 hydroxylation, reduced translation, context-dependent growth arrest, and altered mRNA splicing, with implications for cancer, cardiac biology, and stress adaptation. OGFOD1's unique role in ribosome function distinguishes it among the oxygenase family, and it is considered a therapeutic and research target for modulation of translation and stress pathways.

Other names

2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1KIAA1612TPA1FLJ10826Termination and polyadenylation 1 homologuS12 prolyl 3-hydroxylase

Inhibition of OGFOD1 reduces prolyl hydroxylation of ribosomal protein RPS23, leading to translational arrest, reduced protein synthesis, stress granule formation, and downstream cellular stress responses. Inhibition can also lead to altered splicing patterns by reducing translation of specific splicing regulators