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TRIM3 exacerbates chondrocyte apoptosis through suppression of AKT/mTOR signaling pathway in osteoarthritis. [PDF]
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Emerging Role of TRIM Family Proteins in Cardiovascular Disease
Cardiology, 2020Ubiquitination is one of the basic mechanisms of cell protein homeostasis and degradation and is accomplished by 3 enzymes, E1, E2, and E3. Tripartite motif-containing proteins (TRIMs) constitute the largest subfamily of RING E3 ligases, with >70 current members in humans and mice.
Jing-Rui, Zhang +3 more
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TRIM family proteins: retroviral restriction and antiviral defence
Nature Reviews Microbiology, 2005Members of the tripartite motif (TRIM) protein family are involved in various cellular processes, including cell proliferation, differentiation, development, oncogenesis and apoptosis. Some TRIM proteins display antiviral properties, targeting retroviruses in particular. The potential activity of TRIM19, better known as promyelocytic leukaemia protein,
Sébastien, Nisole +2 more
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The role of TRIM family proteins in autophagy, pyroptosis, and diabetes mellitus
Cell Biology International, 2021AbstractThe ubiquitin‐proteasome system, which is one of the systems for cell protein homeostasis and degradation, happens through the ordered and coordinated action of three types of enzymes, E1 ubiquitin‐activating enzyme, E2 ubiquitin‐carrier enzyme, E3 ubiquitin‐protein ligase.
Tingting Wan, Xiudan Li, Yanbo Li
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The interplay between viruses and TRIM family proteins
Reviews in Medical Virology, 2019SummaryNovel therapeutic options are urgently needed to improve the global treatment of viral infections. Tripartite motif (TRIM) family proteins are involved in various biological and cellular functions including differentiation, development, proliferation, oncogenesis, innate immunity, and viral autophagy.
Ramisha Khan +3 more
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Tumor suppressor p53 and TRIM family proteins
Cancer Cell & Microenvironment, 2015Tumor suppressor p53 plays a key role in maintaining genomic stability and tumor suppression. As a transcription factor, p53 mainly exerts its function in tumor suppression through transcriptional regulation of its target genes to regulate a wide variety of cellular responses. To maintain its proper function, p53 protein levels and activity are tightly
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Diabetes, Obesity and Metabolism, 2023
Abstract Emerging evidence suggests that the ubiquitin‐mediated degradation of insulin‐signalling‐related proteins may be involved in the development of insulin resistance and its related disorders. Tripartite motif‐containing (TRIM) proteins, a superfamily belonging to the E3 ubiquitin ligases, are capable of controlling protein ...
Jianrong Chen +3 more
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Abstract Emerging evidence suggests that the ubiquitin‐mediated degradation of insulin‐signalling‐related proteins may be involved in the development of insulin resistance and its related disorders. Tripartite motif‐containing (TRIM) proteins, a superfamily belonging to the E3 ubiquitin ligases, are capable of controlling protein ...
Jianrong Chen +3 more
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TRIM Family Proteins: Roles in Autophagy, Immunity, and Carcinogenesis
Trends in Biochemical Sciences, 2017Tripartite motif (TRIM) family proteins, most of which have E3 ubiquitin ligase activities, have various functions in cellular processes including intracellular signaling, development, apoptosis, protein quality control, innate immunity, autophagy, and carcinogenesis.
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Inhibition of Retroviral Replication by Members of the TRIM Protein Family
2013The TRIM protein family is emerging as a central component of mammalian antiviral innate immunity. Beginning with the identification of TRIM5α as a mammalian post-entry restriction factor against retroviruses, to the repeated observation that many TRIMs ubiquitinate and regulate signaling pathways, the past decade has witnessed an intense research ...
Adam J, Fletcher, Greg J, Towers
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Structural characterization of TRIM family proteins
2018TRIM proteins are E3 ubiquitin ligases that participate in many cellular processes and signaling pathways, such as immune system response. Several TRIM proteins were shown to form antiparallel coiled-coil dimers which position catalytic RING domains on the opposite sides of an elongated rod. As RING dimerization is necessary for its enzymatic activity,
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