Ubiquitination and deubiquitination in the regulation of N6-methyladenosine functional molecules
- PMID: 38289385
- DOI: 10.1007/s00109-024-02417-9
Ubiquitination and deubiquitination in the regulation of N6-methyladenosine functional molecules
Abstract
N6 methyladenosine (m6A) is the most prevalent RNA epigenetic modification, regulated by methyltransferases and demethyltransferases and recognized by methylation-related reading proteins to impact mRNA splicing, translocation, stability, and translation efficiency. It significantly affects a variety of activities, including stem cell maintenance and differentiation, tumor formation, immune regulation, and metabolic disorders. Ubiquitination refers to the specific modification of target proteins by ubiquitin molecule in response to a series of enzymes. E3 ligases connect ubiquitin to target proteins and usually lead to protein degradation. On the contrary, deubiquitination induced by deubiquitinating enzymes (DUBs) can separate ubiquitin and regulate the stability of protein. Recent studies have emphasized the potential importance of ubiquitination and deubiquitination in controlling the function of m6A modification. In this review, we discuss the impact of ubiquitination and deubiquitination on m6A functional molecules in diseases, such as metabolism, cellular stress, and tumor growth.
Keywords: Degradation; Deubiquitination; RNA modification; Ubiquitination; m6A.
© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
Similar articles
-
The emerging role of deubiquitination in nucleotide excision repair.DNA Repair (Amst). 2016 Aug;44:118-122. doi: 10.1016/j.dnarep.2016.05.035. Epub 2016 Jun 2. DNA Repair (Amst). 2016. PMID: 27316462 Free PMC article. Review.
-
The role of ubiquitination and deubiquitination in tumor invasion and metastasis.Int J Biol Sci. 2022 Mar 6;18(6):2292-2303. doi: 10.7150/ijbs.69411. eCollection 2022. Int J Biol Sci. 2022. PMID: 35414786 Free PMC article. Review.
-
The role of ubiquitination and deubiquitination in the regulation of cell junctions.Protein Cell. 2018 Sep;9(9):754-769. doi: 10.1007/s13238-017-0486-3. Epub 2017 Oct 27. Protein Cell. 2018. PMID: 29080116 Free PMC article. Review.
-
Regulation of Wnt Signaling through Ubiquitination and Deubiquitination in Cancers.Int J Mol Sci. 2020 May 30;21(11):3904. doi: 10.3390/ijms21113904. Int J Mol Sci. 2020. PMID: 32486158 Free PMC article. Review.
-
Programmed Death Ligand 1 Regulatory Crosstalk with Ubiquitination and Deubiquitination: Implications in Cancer Immunotherapy.Int J Mol Sci. 2024 Mar 3;25(5):2939. doi: 10.3390/ijms25052939. Int J Mol Sci. 2024. PMID: 38474186 Free PMC article. Review.
Cited by
-
Deubiquitinase USP5 regulates RIPK1 driven pyroptosis in response to myocardial ischemic reperfusion injury.Cell Commun Signal. 2024 Sep 30;22(1):466. doi: 10.1186/s12964-024-01853-x. Cell Commun Signal. 2024. PMID: 39350285 Free PMC article.
-
Construction of RNA m6A profiles in liver tissue of mice in sepsis-induced liver injury based on m6A MeRIP-seq and RNA-seq.Eur J Med Res. 2025 Aug 8;30(1):723. doi: 10.1186/s40001-025-02985-7. Eur J Med Res. 2025. PMID: 40775729 Free PMC article.
-
Mechanistic Insights and Therapeutic Potentials of Ubiquitin-Proteasome System in Non-Small Cell Lung Cancer.Cell Prolif. 2025 Jul;58(7):e70050. doi: 10.1111/cpr.70050. Epub 2025 May 1. Cell Prolif. 2025. PMID: 40313038 Free PMC article. Review.
-
The role of RNA binding proteins in cancer biology: A focus on FMRP.Genes Dis. 2024 Dec 21;12(4):101493. doi: 10.1016/j.gendis.2024.101493. eCollection 2025 Jul. Genes Dis. 2024. PMID: 40271197 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Medical