IndraLab

Statements

USP12 leads to the ubiquitination of PPM1B. 3 / 3
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"The substrate of USP12, protein phosphatase magnesium-dependent 1B (PPM1B), acts as a phosphatase for IκB kinase β (IKKβ); thus, downregulation of USP12 can accelerate PPM1B ubiquitination and degradation, promoting NF-κB activation and influencing the immune microenvironment."
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"In Kras -driven lung cancer, USP12 suppression, triggered by AKT-mTOR signaling, leads to inadequate deubiquitination of PPM1B, resulting in NF-κB signaling hyperactivation and the creation of an immune-suppressive milieu."
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"USP12 downregulation in tumour cells accelerates PPM1B ubiquitination and degradation and therefore promotes NF-κB activity in orchestrating the TME."
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