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YDJC is a human enzyme predicted to catalyze the deacetylation of acetylated carbohydrates, facilitating degradation of oligosaccharides and binding magnesium ions as a cofactor. In cancer biology, YDJC is upregulated during sphingosylphosphorylcholine (SPC)-induced EMT and promotes reorganization and phosphorylation of keratin 8 (K8), facilitating cell migration and invasion, especially in lung cancer cells. Loss of its deacetylase activity (as in the D13A mutant) abrogates these functions. YDJC interacts with CDC16, a negative regulator of keratin reorganization; when CDC16 is downregulated, YDJC’s promotion of EMT and metastatic phenotypes is more pronounced. Overexpression of YDJC correlates with poor prognosis in lung cancer patients, suggesting its utility as a biomarker and therapeutic target.
For putative drugs targeting YDJC, predicted mechanisms include inhibition of its deacetylase activity, which would block keratin reorganization, EMT, and cancer cell metastasis.
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