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Updated: May 11, 2026
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Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
TRIM proteins as RING finger E3 ubiquitin ligases
Kazuhiro Ikeda1, Satoshi Inoue
1Division of Gene Regulation and Signal Transduction, Research Centerfor Genomic Medicine, Saitama Medical University, Saitama, Japan.
Advances in Experimental Medicine and Biology
|May 1, 2013
Summary
Tripartite motif (TRIM) proteins are crucial for cell growth, immunity, and disease. This chapter explores their role as E3 ubiquitin ligases, highlighting their function in protein degradation pathways.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Tripartite motif (TRIM) proteins, characterized by RING finger, B-box, and coiled-coil (RBCC) domains, constitute a large protein family.
- These proteins are implicated in diverse biological processes such as cell growth, differentiation, apoptosis, and transcription, as well as in disease and oncogenesis.
- Recent research highlights the significant role of TRIM proteins in innate antiviral immunity.
Purpose of the Study:
- To provide a focused overview of the TRIM protein family.
- To specifically examine the function of TRIM proteins as E3 ubiquitin ligases.
- To elucidate the mechanisms underlying TRIM-mediated E3 ligase activity in protein degradation.
Main Methods:
- Review of existing literature on TRIM proteins and their functions.
- Analysis of studies investigating TRIM protein involvement in ubiquitin-mediated protein degradation.
- Focus on the E3 ligase activity of TRIM proteins.
Main Results:
- TRIM proteins are involved in essential cellular processes and disease.
- Some TRIM proteins function as E3 ubiquitin ligases.
- The precise mechanisms of TRIM protein E3 ligase activity require further elucidation.
Conclusions:
- TRIM proteins are versatile regulators with critical roles in cellular functions and immunity.
- Understanding their E3 ligase activity is key to deciphering their biological roles and therapeutic potential.
- Further research is needed to fully elucidate the mechanisms of TRIM-mediated ubiquitination.
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