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Updated: Jul 12, 2025
09:47
Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
Published on: May 10, 2022
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Mutual regulation between TRIM21 and TRIM8 via K48-linked ubiquitination
Lin Wang1, Hui Li1, Aixue Huang1
1Beijing Institute of Basic Medical Sciences, 100850, Beijing, China.
Oncogene
|November 2, 2023
Summary
This study reveals a direct mutual regulation between TRIM21 and TRIM8 in cancer cells, impacting tumor progression and potentially offering new therapeutic strategies for lung and renal cancers.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Tripartite motif (TRIM)-containing proteins are crucial E3 ubiquitin ligases regulating vital cellular processes.
- The mutual regulation among TRIM family members, particularly in cancer, remains largely unexplored.
- TRIM proteins play significant roles in apoptosis, autophagy, immunity, and tumorigenesis.
Purpose of the Study:
- To investigate the potential mutual regulation between TRIM21 and TRIM8 in cancer.
- To elucidate the mechanism underlying the interaction between TRIM21 and TRIM8.
- To explore the clinical relevance of TRIM21 and TRIM8 expression in non-small cell lung cancer (NSCLC) and renal cell carcinoma (RCC).
Main Methods:
- Investigated direct mutual regulation between TRIM21 and TRIM8 in lung and renal cancer cell lines.
- Utilized Lys48 (K48)-linked ubiquitination assays to determine the mechanism of proteasome pathway activation.
- Analyzed the correlation between TRIM21 and TRIM8 expression levels in clinical NSCLC and RCC tissues.
Main Results:
- Demonstrated a direct mutual regulation between TRIM21 and TRIM8 in cancer cells.
- Identified activation of the proteasome pathway via K48-linked ubiquitination as the underlying mechanism.
- Observed negatively correlated expressions of TRIM21 and TRIM8 in clinical NSCLC and RCC tissues, associated with tumor progression.
Conclusions:
- Established a novel mutual regulatory mechanism between TRIM21 and TRIM8 in cancer.
- Highlighted a potential homeostasis between TRIM21 and TRIM8 that may influence cancer stemness.
- Suggested that this interaction could offer new avenues for cancer therapy development.
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