Emerging RNA-binding roles in the TRIM family of ubiquitin ligases-Reference-Cited by-同舟云学术

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

Published:2019-05-23 Issue:11 Volume:400 Page:1443-1464
ISSN:1437-4315
Container-title:Biological Chemistry
language:en
Short-container-title:

Author:

Williams Felix Preston¹²,Haubrich Kevin¹²,Perez-Borrajero Cecilia¹,Hennig Janosch³^ORCID

Affiliation:

1. Structural and Computational Biology Unit , European Molecular Biology Laboratory (EMBL) , Heidelberg , Germany

2. Collaboration for Joint PhD Degree between EMBL and Heidelberg University , Faculty of Biosciences , Heidelberg , Germany

3. Structural and Computational Biology Unit , European Molecular Biology Laboratory (EMBL) , Heidelberg , Germany , e-mail:

Abstract

Abstract 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.

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Biology,Biochemistry

Reference188 articles.

1. Aeschimann, F., Kumari, P., Bartake, H., Gaidatzis, D., Xu, L., Ciosk, R., and Grosshans, H. (2017). LIN41 post-transcriptionally silences mRNAs by two distinct and position-dependent mechanisms. Mol. Cell 65, 476–489.

2. Ahmad, Y. and Lamond, A.I. (2014). A perspective on proteomics in cell biology. Trends Cell Biol. 24, 257–264.

3. Akutsu, M., Dikic, I., and Bremm, A. (2016). Ubiquitin chain diversity at a glance. J. Cell Sci. 129, 875.

4. Albor, A., El-Hizawi, S., Horn, E.J., Laederich, M., Frosk, P., Wrogemann, K., and Kulesz-Martin, M. (2006). The interaction of piasy with TRIM32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB. J. Biol. Chem. 281, 25850–25866.

5. Ali, H., Mano, M., Braga, L., Naseem, A., Marini, B., Vu, D.M., Collesi, C., Meroni, G., Lusic, M., and Giacca, M. (2019). Cellular TRIM33 restrains HIV-1 infection by targeting viral integrase for proteasomal degradation. Nat. Commun. 10, 926.

Cited by 48 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Identification of a novel ferroptosis-inducing micropeptide in bladder cancer;Cancer Letters;2024-02

2. It’s a TRIM-endous view from the top: the varied roles of TRIpartite Motif proteins in brain development and disease;Frontiers in Molecular Neuroscience;2023-12-05

3. Patterns of Evolution of TRIM Genes Highlight the Evolutionary Plasticity of Antiviral Effectors in Mammals;Genome Biology and Evolution;2023-11-21

4. Genome-wide mapping of regulatory variants for temperature- and salinity-adaptive genes reveals genetic basis of genotype-by-environment interaction in Crassostrea ariakensis;Environmental Research;2023-11

5. Role of the tripartite motif (TRIM) family in female genital neoplasms;Pathology - Research and Practice;2023-10