Emerging RNA-binding roles in the TRIM family of ubiquitin ligases - PubMed (original) (raw)

Review

. 2019 Oct 25;400(11):1443-1464.

doi: 10.1515/hsz-2019-0158.

Affiliations

• PMID: 31120853
• DOI: 10.1515/hsz-2019-0158

Free article

Review

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

Felix Preston Williams et al. Biol Chem. 2019.

Free article

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.

Keywords: NHL domains; PRY/SPRY domains; RNA-binding; TRIM proteins; TRIM25; ubiquitination.

PubMed Disclaimer

Similar articles

• RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination.
  Choudhury NR, Heikel G, Trubitsyna M, Kubik P, Nowak JS, Webb S, Granneman S, Spanos C, Rappsilber J, Castello A, Michlewski G. Choudhury NR, et al. BMC Biol. 2017 Nov 8;15(1):105. doi: 10.1186/s12915-017-0444-9. BMC Biol. 2017. PMID: 29117863 Free PMC article.
• TRIM-NHL as RNA Binding Ubiquitin E3 Ligase (RBUL): Implication in development and disease pathogenesis.
  Goyani S, Roy M, Singh R. Goyani S, et al. Biochim Biophys Acta Mol Basis Dis. 2021 Jul 1;1867(7):166066. doi: 10.1016/j.bbadis.2020.166066. Epub 2021 Jan 6. Biochim Biophys Acta Mol Basis Dis. 2021. PMID: 33418035 Review.
• TRIM proteins as RING finger E3 ubiquitin ligases.
  Ikeda K, Inoue S. Ikeda K, et al. Adv Exp Med Biol. 2012;770:27-37. doi: 10.1007/978-1-4614-5398-7_3. Adv Exp Med Biol. 2012. PMID: 23630998 Review.
• Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity.
  Bhaduri U, Merla G. Bhaduri U, et al. Cells. 2021 Apr 25;10(5):1015. doi: 10.3390/cells10051015. Cells. 2021. PMID: 33923045 Free PMC article. Review.
• TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity.
  Gack MU, Shin YC, Joo CH, Urano T, Liang C, Sun L, Takeuchi O, Akira S, Chen Z, Inoue S, Jung JU. Gack MU, et al. Nature. 2007 Apr 19;446(7138):916-920. doi: 10.1038/nature05732. Nature. 2007. PMID: 17392790

Cited by

• The Role of Ubiquitination in Osteosarcoma Development and Therapies.
  Mao P, Feng Z, Liu Y, Zhang K, Zhao G, Lei Z, Di T, Zhang H. Mao P, et al. Biomolecules. 2024 Jul 3;14(7):791. doi: 10.3390/biom14070791. Biomolecules. 2024. PMID: 39062505 Free PMC article. Review.
• The mTOR regulated RNA-binding protein LARP1 requires PABPC1 for guided mRNA interaction.
  Smith EM, Benbahouche NEH, Morris K, Wilczynska A, Gillen S, Schmidt T, Meijer HA, Jukes-Jones R, Cain K, Jones C, Stoneley M, Waldron JA, Bell C, Fonseca BD, Blagden S, Willis AE, Bushell M. Smith EM, et al. Nucleic Acids Res. 2021 Jan 11;49(1):458-478. doi: 10.1093/nar/gkaa1189. Nucleic Acids Res. 2021. PMID: 33332560 Free PMC article.
• A novel role of TRIM28 B box domain in L1 retrotransposition and ORF2p-mediated cDNA synthesis.
  Du Q, Stow EC, LaCoste D, Freeman B, Baddoo M, Shareef AM, Miller KM, Belancio VP. Du Q, et al. Nucleic Acids Res. 2023 May 22;51(9):4429-4450. doi: 10.1093/nar/gkad247. Nucleic Acids Res. 2023. PMID: 37070200 Free PMC article.
• TRIM32: A Multifunctional Protein Involved in Muscle Homeostasis, Glucose Metabolism, and Tumorigenesis.
  Bawa S, Piccirillo R, Geisbrecht ER. Bawa S, et al. Biomolecules. 2021 Mar 10;11(3):408. doi: 10.3390/biom11030408. Biomolecules. 2021. PMID: 33802079 Free PMC article. Review.
• Cytoplasmic RNA sensors and their interplay with RNA-binding partners in innate antiviral response: theme and variations.
  Chan CP, Jin DY. Chan CP, et al. RNA. 2022 Apr;28(4):449-477. doi: 10.1261/rna.079016.121. Epub 2022 Jan 14. RNA. 2022. PMID: 35031583 Free PMC article. Review.

References

1. 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. 1. Ahmad, Y. and Lamond, A.I. (2014). A perspective on proteomics in cell biology. Trends Cell Biol. 24, 257–264.
3. 1. Akutsu, M., Dikic, I., and Bremm, A. (2016). Ubiquitin chain diversity at a glance. J. Cell Sci. 129, 875.
4. 1. 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. 1. 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.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • De Gruyter