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The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.

ABSTRACT: Ubiquitin-specific peptidase 24 (USP24), a cysteine protease, functions as deubiquitinating enzyme that recognizes and removes ubiquitin from the target protein. USP24 is overexpressed in various cancers and regulates the stability of proteins involved in cancer metastasis, cancer stemness, and drug resistance. While the expression profile alteration in tumor microenvironment upon USP24 inhibition is unrevealed. Through RNA-seq, we have characterized that USP24 catalytically inactivation upregulates activation of immune response and lymphocyte activation-related genes in lung tumors from EgfrL858RUsp24C1695A mice

ORGANISM(S): Mus musculus

PROVIDER: GSE281983 | GEO | 2025/04/22

REPOSITORIES: GEO

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Project description:Pseudomonas aeruginosa is a human pathogen that relies on quorum sensing to establish infections. The PqsE quorum-sensing protein is required for P. aeruginosa virulence factor production and infection. PqsE has a reported enzymatic function in the biosynthesis of the quorum-sensing autoinducer called PQS. However, this activity is redundant because, in the absence of PqsE, this role is fulfilled by alternative thioesterases. Rather, PqsE drives P. aeruginosa pathogenic traits via a protein-protein interaction with the quorum-sensing receptor/transcription factor RhlR, an interaction that enhances the affinity of RhlR for target DNA sequences. PqsE catalytic activity is dispensable for interaction with RhlR. Thus, the virulence function of PqsE can be decoupled from its catalytic function. Here, we present an immunoprecipitation-mass spectrometry method employing enhanced green fluorescent protein-PqsE fusions to define the protein interactomes of wild-type PqsE and the catalytically inactive PqsE(D73A) variant in P. aeruginosa and their dependence on RhlR. Several proteins were identified to have specific interactions with wild-type PqsE while not forming associations with PqsE(D73A). In the ΔrhlR strain, an increased number of specific PqsE interactors were identified, including the partner autoinducer synthase for RhlR, called RhlI. Collectively, these results suggest that specific protein-protein interactions depend on PqsE catalytic activity and that RhlR may prevent proteins from interacting with PqsE, possibly due to competition between RhlR and other proteins for PqsE binding. Our results provide a foundation for the identification of the in vivo PqsE catalytic function and, potentially, new proteins involved in P. aeruginosa quorum sensing. IMPORTANCE Pseudomonas aeruginosa causes hospital-borne infections in vulnerable patients, including immunocompromised individuals, burn victims, and cancer patients undergoing chemotherapy. There are no effective treatments for P. aeruginosa infections, which are usually broadly resistant to antibiotics. Animal models show that, to establish infection and to cause illness, P. aeruginosa relies on an interaction between two proteins, namely, PqsE and RhlR. There could be additional protein-protein interactions involving PqsE, which, if defined, could be exploited for the design of new therapeutic strategies to combat P. aeruginosa. Here, we reveal previously unknown protein interactions in which PqsE participates, which will be investigated for potential roles in pathogenesis.

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The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.

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