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TRAIP suppresses bladder cancer progression by catalyzing K48-linked polyubiquitination of MYC

ABSTRACT: TRAIP suppresses bladder cancer progression by catalyzing K48-linked polyubiquitination of MYC

PROVIDER: PRJNA993280 | ENA |

REPOSITORIES: ENA

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TRAIP suppresses bladder cancer progression by catalyzing K48-linked polyubiquitination of MYC

Project description:Tumor necrosis factor (TNF) receptor-associated factor (TRAF)-interacting protein (TRAIP), a RING domain-containing E3 ligase, has emerged as a key player in safeguarding genome integrity and is closely linked to cancer. Here, we discovered that TRAIP exhibits low expression in bladder cancer (BLCA), which correlates with poor prognosis. TRAIP exerts inhibitory effects on bladder cancer cell proliferation and migration both in vitro and in vivo. MYC serves as a newly identified target for TRAIP, with direct interaction leading to the promotion of K48 polyubiquitination at K428/430 lysine residues, subsequently resulting in proteasome-dependent degradation and downregulation of MYC's transcriptional activity. This process effectively hinders the progression of bladder cancer. Restoration of MYC expression rescues the suppressed proliferation and migration of bladder cancer cells induced by TRAIP. Furthermore, our investigation also demonstrates that MYC binds to the transcriptional start region of TRAIP, exerting regulatory control over TRAIP transcription. Consequently, this interaction establishes a negative feedback loop that prevents excessive expression of MYC. In summary, our study uncovers a novel mechanism by which TRAIP inhibits the progression of bladder cancer through the ubiquitinated degradation of MYC.

2023-12-28 | GSE237002 | GEO

Pcgf6 suppresses Myc-induced lymphomagenesis

Project description:Pcgf6 suppresses Myc-induced lymphomagenesis

| PRJNA785557 | ENA

miR-193 inhibits bladder cancer progression by targeting N-myc

Project description:Growing evidence has indicated that miR-193 is involved in the initiation and progression of malignancy, such as bladder cancer, hepatocellular carcinoma, renal cell carcinoma, and colorectal cancer. Nevertheless, the mechanisms of miR-193 in the development of metastatic bladder cancer remains unknown. In the current study, we clarified the association of miR-193/N-myc was implicated in cancer metastasis. miR-193 expression increased in metastatic bladder cancer biopsies compared to the primary cases. Moreover, the elevation of miR-193 was correlated with the invasiveness, lymph node metastasis, and advanced stages of bladder cancer significantly. Downregulation of miR-193 by shRNA hampered proliferation and migration while inducing cell apoptosis. Furthermore, miR-193 sponged N-myc and diminished miR-103 expression. Overexpression of miR-193 released oncogene N-myc expression, leading to the promotion of cell proliferation and migration. Besides, knockout of miR-193 suppressed tumor growth in the human T24 mice models. Briefly, the present findings suggested that miR-193-N-myc were novel promising pathways for conquering bladder cancer progression.

2021-01-13 | GSE164682 | GEO

DNA polymerase POLD1 promotes proliferation and metastasis of bladder cancer by stabilizing MYC

Project description:Hitherto, most studies on POLD1 have mainly focused on the effect of POLD1 inactivation mutation in tumors. Nonetheless, the mechanism underlying high POLD1 expression in tumorigenesis remains elusive. Herein, we substantiated the pro-carcinogenic role of POLD1 in bladder cancer (BLCA) and found that POLD1 expression is related to malignancy and prognosis of BLCA. Next, we demonstrated that POLD1 could promote proliferation and metastasis of BLCA via MYC. Mechanistically, we demonstrated that POLD1 was able to stabilize MYC in a manner independent of DNA polymerase activity. POLD1 attenuated the FBXW7-mediated ubiquitination degradation of MYC by directly binding to the MYC homology box 1 domain competitively with FBXW7. Moreover, we found that POLD1 can form a complex with MYC to promote the transcriptional activity of MYC. MYC could also transcriptionally activate POLD1, forming a POLD1-MYC positive feedback loop to enhance the pro-carcinogenic effect of POLD1-MYC on BLCA. Overall, our study suggests a novel MYC-driven mechanism for BLCA, and POLD1 has the potential as a biomarker for BLCA.

2023-03-29 | PXD040806 | Pride

CircNCOR1 suppresses lymphatic metastasis in bladder cancer

Project description:CircNCOR1 suppresses lymphatic metastasis in bladder cancer

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Pcgf6 suppresses Myc-induced lymphomagenesis [RNA-seq]

Project description:Pcgf6 suppresses Myc-induced lymphomagenesis [RNA-seq]

| PRJNA785559 | ENA

Pcgf6 suppresses Myc-induced lymphomagenesis [ChIP-seq]

Project description:Pcgf6 suppresses Myc-induced lymphomagenesis [ChIP-seq]

| PRJNA785540 | ENA

Polyubiquitination analysis upon GSK3 inhibition in HeLa cell extracts

Project description:HeLa cell extracts with or without GSK3 enzyme inhibition were assayed using protein microarrays in order to detect GSK3-dependent changes in protein polyubiquitination. HeLa lysates in triplicates were supplemented with ubiquitin and incubated on protein microarrays (ProtoArray 5.0; Invitrogen) in the presence or absence of the GSK3 inhibitor SB-216763. Polyubiquitination of the arrayed proteins was detected using specific antibodies. ProtoArray 5.0 contains over 9,000 full-length human proteins purified and arrayed in duplicate under native conditions to maximize functionality.

2014-05-15 | E-GEOD-50629 | biostudies-arrayexpress

JOSD2 promotes non-small cell lung cancer proliferation by removing K6-linked polyubiquitination from LKB1

Project description:JOSD2 promotes non-small cell lung cancer proliferation by removing K6-linked polyubiquitination from LKB1

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TRIM37 augments AP-2γ transcriptional activity and cellular localization via K63-linked polyubiquitination to drive breast cancer progression [ChIP-seq]

Project description:Using a proteomics approach, we identified the Tripartite Motif Containing 37 (TRIM37) as a novel transcriptional coactivator of AP-2γ. We demonstrate TRIM37 facilitates AP-2γ chromatin binding to regulate the AP-2γ mediated transcriptional program directly. We provide evidence that TRIM37 achieves this by stimulating K63-chain-linked polyubiquitination of AP-2γ, promoting protein localization from the cytoplasm to the nucleus. In clinical analyses, we find TRIM37 is upregulated in multiple breast cancer datasets, supporting our findings that TRIM37-AP-2γ interaction is essential for breast cancer tumor growth. Overall, our work revealed that TRIM37 is an oncogenic coactivator of AP-2γ in breast cancer and provides a novel therapeutic target for treating the disease.

2022-07-25 | GSE182546 | GEO

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