Atypical K6-ubiquitin chains mobilize p97/VCP and the proteasome to resolve formaldehyde-induced RNA-protein crosslinks
- PMID: 38065058
- DOI: 10.1016/j.molcel.2023.11.009
Atypical K6-ubiquitin chains mobilize p97/VCP and the proteasome to resolve formaldehyde-induced RNA-protein crosslinks
Abstract
In this issue of Molecular Cell, Rahmanto et al.1 and Zhao et al.2 demonstrate that RNA-protein crosslinks contribute to formaldehyde toxicity by blocking protein synthesis. Furthermore, they identify a ubiquitin-mediated degradation system for RNA-protein crosslink resolution in eukaryotes.
Copyright © 2023 Elsevier Inc. All rights reserved.
Conflict of interest statement
Declaration of interests The authors declare no competing interests.
Comment on
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K6-linked ubiquitylation marks formaldehyde-induced RNA-protein crosslinks for resolution.Mol Cell. 2023 Dec 7;83(23):4272-4289.e10. doi: 10.1016/j.molcel.2023.10.011. Epub 2023 Nov 10. Mol Cell. 2023. PMID: 37951215
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RNF14-dependent atypical ubiquitylation promotes translation-coupled resolution of RNA-protein crosslinks.Mol Cell. 2023 Dec 7;83(23):4290-4303.e9. doi: 10.1016/j.molcel.2023.10.012. Epub 2023 Nov 10. Mol Cell. 2023. PMID: 37951216 Free PMC article.
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