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An E3 ligase TRIM1 promotes colorectal cancer progression via K63-linked ubiquitination and activation of HIF1α

ABSTRACT: We determined the binding and ubiquitination of HIF1a by an E3 ligase TRIM1. IP experiments were performed from SW480 cells and Ms files were acquired on Q Exactive mass spectrometer. We analysed the differences of protein abundance, comparing the normalized intensity on distinct proteins from different groups.

ORGANISM(S): Homo Sapiens

SUBMITTER: Kun Meng

PROVIDER: PXD046557 | iProX | Thu Feb 22 00:00:00 GMT 2024

REPOSITORIES: iProX

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An E3 ligase TRIM1 promotes colorectal cancer progression via K63-linked ubiquitination and activation of HIF1α.

Shi Liuliu L Fang Xianglan X Du Lijie L Yang Jin J Xue Juan J Yue Xiaokai X Xie Duoshuang D Hui Yuanjian Y Meng Kun K

Oncogenesis 20240520 1

Accumulating studies have shown that E3 ligases play crucial roles in regulating cellular biological processes and signaling pathways during carcinogenesis via ubiquitination. Tripartite-motif (TRIM) ubiquitin E3 ligases consist of over 70 members. However, the clinical significance and their contributions to tumorigenesis remain largely unknown. In this study, we analyzed the RNA-sequencing expression of TRIM E3 ligases in colorectal cancer (CRC) and identified 10 differentially expressed genes ...[more]

PMID: 38769340

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