AI Article Synopsis
- Ribosomes are influenced by ubiquitination and deubiquitination processes, with the deubiquitinase OTUD6 playing a key role in protein translation in Drosophila by modifying the RPS7 subunit of the 40S ribosome.
- Research shows that OTUD6 interacts specifically with the free 40S ribosomes and that several proteins, including RACK1 and E3 ligases like CNOT4 and RNF10, are involved in regulating this interaction and responding to cellular stress.
- The levels of OTUD6 can change due to aging and stress, suggesting it helps control the initiation of protein translation by affecting the recycling of the 40S ribosomes.
Article Abstract
Ribosomes are regulated by evolutionarily conserved ubiquitination/deubiquitination events. We uncover the role of the deubiquitinase OTUD6 in regulating global protein translation through deubiquitination of the RPS7/eS7 subunit on the free 40 S ribosome in vivo in Drosophila. Coimmunoprecipitation and enrichment of monoubiquitinated proteins from catalytically inactive OTUD6 flies reveal RPS7 as the ribosomal substrate. The 40 S protein RACK1 and E3 ligases CNOT4 and RNF10 function upstream of OTUD6 to regulate alkylation stress. OTUD6 interacts with RPS7 specifically on the free 40 S, and not on 43 S/48 S initiation complexes or the translating ribosome. Global protein translation levels are bidirectionally regulated by OTUD6 protein abundance. OTUD6 protein abundance is physiologically regulated in aging and in response to translational and alkylation stress. Thus, OTUD6 may promote translation initiation, the rate limiting step in protein translation, by titering the amount of 40 S ribosome that recycles.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11316749 | PMC |
| http://dx.doi.org/10.1038/s41467-024-51284-y | DOI Listing |
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