Journal
NATURE COMMUNICATIONS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms9670
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Funding
- Wellcome Trust [084957/Z/08/Z]
- Biotechnology and Biological Sciences Research Council [ISPG BBS/E/B/000C0409]
- Cambridge Biomedical Research Centre (UK)
- Wellcome Trust [084957/Z/08/Z] Funding Source: Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BBS/E/B/000C0409, BBS/E/B/000C0407, BB/J00152X/1, BB/E02338X/1] Funding Source: researchfish
- BBSRC [BBS/E/B/000C0409, BB/E02338X/1, BB/J00152X/1, BBS/E/B/000C0407] Funding Source: UKRI
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The regulation of protein and mRNA turnover is essential for many cellular processes. We recently showed that ubiquitin-traditionally linked to protein degradation-directly regulates the degradation of mRNAs through the action of a newly identified family of RNA-binding E3 ubiquitin ligases. How ubiquitin regulates mRNA decay remains unclear. Here, we identify a new role for ubiquitin in regulating deadenylation, the initial and often rate-limiting step in mRNA degradation. MEX-3C, a canonical member of this family of RNA-binding ubiquitin ligases, associates with the cytoplasmic deadenylation complexes and ubiquitinates CNOT7(Caf1), the main catalytic subunit of the CCR4-NOT deadenylation machinery. We establish a new role for ubiquitin in regulating MHC-I mRNA deadenylation as ubiquitination of CNOT7 by MEX-3C regulates its deadenylation activity and is required for MHC-I mRNA degradation. Since neither proteasome nor lysosome inhibitors rescued MEX-3C-mediated MHC-I mRNA degradation, our findings suggest a new non-proteolytic function for ubiquitin in the regulation of mRNA decay.
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