Literature by the same author
plus at Google Scholar

Bibliografische Daten exportieren
 

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

Title data

Williams, Felix Preston ; Haubrich, Kevin ; Perez-Borrajero, Cecilia ; Hennig, Janosch:
Emerging RNA-binding roles in the TRIM family of ubiquitin ligases.
In: Biological Chemistry. Vol. 400 (2019) Issue 11 . - pp. 1443-1464.
ISSN 1437-4315
DOI: https://doi.org/10.1515/hsz-2019-0158

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: NHL domains; PRY/SPRY domains; RNA-binding; TRIM proteins; TRIM25; ubiquitination
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry > Chair Biochemistry IV - Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry IV - Biophysical Chemistry
Research Institutions > Central research institutes > Nordbayerisches Zentrum für NMR-Spektroskopie - NMR-Zentrum
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 06 Oct 2021 11:31
Last Modified: 26 Sep 2024 07:26
URI: https://eref.uni-bayreuth.de/id/eprint/67212