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Published on: May 18, 2020
Altered Expression of TRIM Proteins - Inimical Outcome and Inimitable Oncogenic Function in Breast Cancer with
Suman Kumar Ray1, Sukhes Mukherjee2
1Independent Researcher, Bhopal, Madhya Pradesh, India.
Abstract:
Deregulation of ubiquitin-mediated degradation of oncogene products or tumor suppressors appears to be implicated in the genesis of carcinomas, according to new clinical findings. Conferring to recent research, some members of the tripartite motif (TRIM) proteins (a subfamily of the RING type E3 ubiquitin ligases) act as significant carcinogenesis regulators. Intracellular signaling, development, apoptosis, protein quality control, innate immunity, autophagy, and carcinogenesis are all regulated by TRIM family proteins, the majority of which have E3 ubiquitin ligase activity. The expression of TRIMs in tumors is likely to be related to the formation and/or progression of the disease, and TRIM expression could be used to predict cancer prognosis. Breast cancer is the most common malignancy in women and also the leading cause of death. TRIM family proteins have unique, vital activities, and their dysregulation, such as TRIM 21, promotes breast cancer, according to growing evidence. Many TRIM proteins have been identified as important cancer biomarkers, with decreased or elevated levels of expression. TRIM29 functions as a hypoxia-induced tumor suppressor gene, revealing a new molecular mechanism for ATM-dependent breast cancer suppression. In breast cancer cells, the TRIM28-TWIST1-EMT axis exists, and TRIM28 enhances breast cancer metastasis by stabilizing TWIST1, and thereby increasing epithelial-tomesenchymal transition. Interestingly, many TRIM proteins are involved in the control of p53, and many TRIM proteins are likewise regulated by p53, according to current research. Furthermore, TRIMs linked to specific tumors may aid in the creation of innovative TRIM-targeted cancer treatments. This review focuses on TRIM proteins that are involved in tumor development, progression, and are of clinical significance in breast cancer.
Insights
Tripartite motif (TRIM) proteins, a class of E3 ubiquitin ligases, are crucial regulators in cancer development. Their dysregulation, particularly in breast cancer, highlights their potential as diagnostic biomarkers and therapeutic targets.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Deregulation of protein degradation pathways, specifically ubiquitin-mediated degradation, is implicated in cancer genesis.
- Tripartite motif (TRIM) proteins, a family of RING-type E3 ubiquitin ligases, play significant roles in regulating carcinogenesis.
- TRIM proteins are involved in diverse cellular processes including signaling, development, apoptosis, immunity, and autophagy.
Approach:
- This review synthesizes current research on the involvement of TRIM proteins in tumor development and progression.
- Focuses on the clinical significance of TRIM proteins, particularly in breast cancer.
- Examines specific TRIM proteins like TRIM21, TRIM28, and TRIM29 and their roles in breast cancer pathogenesis.
Key Points:
- TRIM protein expression levels in tumors correlate with disease formation, progression, and prognosis.
- Dysregulation of TRIM proteins, such as TRIM21, promotes breast cancer development.
- TRIM28 facilitates breast cancer metastasis by stabilizing TWIST1 and promoting epithelial-to-mesenchymal transition (EMT).
- TRIM29 acts as a hypoxia-induced tumor suppressor in breast cancer, mediated by ATM.
- Many TRIM proteins interact with and are regulated by the tumor suppressor p53.
Conclusions:
- TRIM proteins are critical regulators in breast cancer, influencing tumor initiation, progression, and metastasis.
- Altered expression of TRIM proteins serves as potential biomarkers for cancer diagnosis and prognosis.
- Targeting specific TRIM proteins offers a promising avenue for developing novel cancer therapies.
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