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Trim45: An emerging E3 ubiquitin ligases in cancer
Huhu Zhang1, Xinping He1, Lina Yang1
1Department of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao 266071, Shandong, China.
Abstract:
The ubiquitin proteasome system is the major pathway for intracellular protein degradation and relies on ATP supply to specifically degrade misfolded or damaged proteins. The system consists of E1, E2, and E3 enzymes that mediate the ubiquitination modification of substrate proteins, followed by proteasomal recognition and degradation of the substrate proteins. The substrate specificity and structural diversity of E3 ubiquitin ligases allow for precise recognition and degradation of proteins by the system. E3 ubiquitin ligases function by specifically recognizing target proteins, and catalyze the transfer of ubiquitin molecules from E2 ubiquitin-conjugating enzymes to substrate proteins. Trim45 is a member of the a member of the triadic motif (Trim) family of proteins that regulate biological processes such as the cell cycle, cell proliferation, apoptosis, and transcription, and are involved in pathological processes such as inflammatory responses and tumour progression. Trim45 is thought to be closely associated with the development and progression of many cancers, including cervical cancer, glioblastoma, non-small cell lung cancer, breast cancer, hepatocellular carcinoma and colon cancer. This review focuses on the mechanism, function, and clinical significance of Trim45 in various cancers and demonstrates that Trim45 is involved in regulating multiple signaling pathways as well as maintaining protein stability. Therefore, Trim45 is a potential biomarker and therapeutic target in tumour therapy, providing reference value for patient prognosis. Subject terms: Trim45, Cancer, Cell biology, Ubiquitination.
Insights
Triadic motif 45 (Trim45) plays a key role in cancer progression by regulating protein stability and signaling pathways. This protein is a potential biomarker and therapeutic target for various tumors, offering insights into patient prognosis.
Area of Science:
- Cell Biology
- Molecular Biology
- Oncology
Background:
- The ubiquitin proteasome system (UPS) is crucial for intracellular protein degradation, utilizing E1, E2, and E3 enzymes for ubiquitination.
- E3 ubiquitin ligases, like Trim45, confer substrate specificity, enabling precise protein degradation and regulation of cellular processes.
- The triadic motif (Trim) family, including Trim45, is implicated in cell cycle, proliferation, apoptosis, and transcription, and linked to cancer development.
Purpose of the Study:
- To review the mechanism, function, and clinical significance of Trim45 in various cancers.
- To highlight Trim45's role in regulating signaling pathways and protein stability.
- To establish Trim45 as a potential biomarker and therapeutic target in oncology.
Main Methods:
- Literature review focusing on Trim45's involvement in cancer.
- Analysis of Trim45's regulatory functions in cellular signaling and protein homeostasis.
- Examination of Trim45's association with cancer development and progression.
Main Results:
- Trim45 is implicated in the pathogenesis of multiple cancers, including cervical, lung, breast, liver, and colon cancers.
- Trim45 regulates key signaling pathways and maintains protein stability, influencing tumor progression.
- Evidence suggests Trim45's involvement in inflammatory responses and tumor growth.
Conclusions:
- Trim45 is a significant factor in cancer development and progression across various tumor types.
- Trim45's functions in regulating protein stability and signaling pathways make it a promising therapeutic target.
- Trim45 holds potential as a prognostic biomarker for cancer patients, guiding treatment strategies.
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