Emerging RNA-binding roles in the TRIM family of ubiquitin ligases

TRIM proteins constitute a large, diverse and ancient protein family which play a key role in processes including cellular differentiation, autophagy, apoptosis, DNA repair, and tumour suppression. Mostly known and studied through the lens of their ubiquitination activity as E3 ligases, it has recen...

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Main Authors: Williams, Felix Preston (Author) , Haubrich, Kevin (Author) , Hennig, Janosch (Author)
Format: Article (Journal)
Language:English
Published: May 23, 2019
In: Biological chemistry
Year: 2019, Volume: 400, Issue: 11, Pages: 1443-1464
ISSN:1437-4315
DOI:10.1515/hsz-2019-0158
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1515/hsz-2019-0158
Verlag, lizenzpflichtig, Volltext: https://www.degruyterbrill.com/view/journals/bchm/400/11/article-p1443.xml
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Author Notes:Felix Preston Williams, Kevin Haubrich, Cecilia Perez-Borrajero and Janosch Hennig
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Summary:TRIM proteins constitute a large, diverse and ancient protein family which play a key role in processes including cellular differentiation, autophagy, apoptosis, DNA repair, and tumour suppression. Mostly known and studied through the lens of their ubiquitination activity as E3 ligases, it has recently emerged that many of these proteins are involved in direct RNA binding through their NHL or PRY/SPRY domains. We summarise the current knowledge concerning the mechanism of RNA binding by TRIM proteins and its biological role. We discuss how RNA-binding relates to their previously described functions such as E3 ubiquitin ligase activity, and we will consider the potential role of enrichment in membrane-less organelles.</p></section>
Item Description:Gesehen am 22.04.2020
Physical Description:Online Resource
ISSN:1437-4315
DOI:10.1515/hsz-2019-0158