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• W2941400325 endingPage "e201900295" @default.
• W2941400325 startingPage "e201900295" @default.
• W2941400325 abstract "TRIM E3 ubiquitin ligases regulate multiple cellular processes, and their dysfunction is linked to disease. They are characterised by a conserved N-terminal tripartite motif comprising a RING, B-box domains, and a coiled-coil region, with C-terminal domains often mediating substrate recruitment. TRIM proteins are grouped into 11 classes based on C-terminal domain identity. Class VI TRIMs, TRIM24, TRIM33, and TRIM28, have been described as transcriptional regulators, a function linked to their C-terminal plant homeodomain and bromodomain, and independent of their ubiquitination activity. It is unclear whether E3 ligase activity is regulated in family members where the C-terminal domains function independently. Here, we provide a detailed biochemical characterisation of the RING domains of class VI TRIMs and describe the solution structure of the TRIM28 RING. Our study reveals a lack of activity of the isolated RING domains, which may be linked to the absence of self-association. We propose that class VI TRIMs exist in an inactive state and require additional regulatory events to stimulate E3 ligase activity, ensuring that associated chromatin-remodelling factors are not injudiciously degraded." @default.
• W2941400325 created "2019-05-03" @default.
• W2941400325 creator A5021310521 @default.
• W2941400325 creator A5030891704 @default.
• W2941400325 creator A5051625670 @default.
• W2941400325 date "2019-04-26" @default.
• W2941400325 modified "2023-09-26" @default.
• W2941400325 title "Characterisation of class VI TRIM RING domains: linking RING activity to C-terminal domain identity" @default.
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• W2941400325 doi "https://doi.org/10.26508/lsa.201900295" @default.
• W2941400325 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6487577" @default.
• W2941400325 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31028095" @default.
• W2941400325 hasPublicationYear "2019" @default.
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