IndraLab

Statements

USP4 activates MAP3K7. 8 / 8
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"Previous study also showed that USP4 targets TAK1 by removing K63 linked polyubiquitination and then recruit IkappaB kinase (IKK) complex to simulate TNF-alpha -induced NF-kappaB activation 49."
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"Taken together, these results indicate that USP4 accelerates ESCC cell progression by targeting TAK1."
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"USP4 directly deubiquitinated transforming growth factor-β activated kinase 1 (TAK1), resulting in TAK1 dephosphorylation [109]."
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"USP4 promotes the proliferation, migration, and invasion of esophageal squamous cell carcinoma by targeting TAK1."
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"In addition, USP4 promotes the proliferation, migration, and invasion of esophageal squamous cell carcinoma by targeting TAK1."
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"The protein expression of USP4 in liver tissue samples from patients with NAFLD was significantly lower than that of healthy controls, and mechanistically, USP4 inhibits TAK1 degradation by removing the K48-linked ubiquitinated chain, leading to inhibition of signaling activation of the downstream NF-κB and JNK cascades, which in turn reverses the disruption of IRS-AKT-GSK3β signaling, inhibits IR, and thus attenuates hepatic steatosis and inflammation (35)."
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"Molecular analysis revealed that USP4 deficiency augmented the activation of the transforming growth factor beta activated kinase 1 (TAK1)-(JNK1/2)/P38 signaling in response to hypertrophic stress, and blockage of TAK1 activation abolished the pathological effects of USP4 deficiency in vivo."
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"Importantly, USP4 dramatically accelerates the malignant phenotype of ESCC cells by targeting TAK1 in ESCC, suggesting that the USP4–TAK1 axis plays an important role in ESCC malignant progression."
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