ArticleCurrent genetics2010
Synthetic lethality of rpn11-1 rpn10Δ is linked to altered proteasome assembly and activity.
Article in Current genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Dosage suppressors of gpn2ts mutants and functional insights into the role of Gpn2 in budding yeast.PloS one · 2024Article
- A novel endoplasmic reticulum adaptation is critical for the long-lived Caenorhabditis elegans rpn-10 proteasomal mutant.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- Activation of the ubiquitin-proteasome system contributes to oculopharyngeal muscular dystrophy through muscle atrophy.PLoS genetics · 2022Article
- Chaperone-mediated 26S proteasome remodeling facilitates free K63 ubiquitin chain production and aggresome clearance.The Journal of biological chemistry · 2015Article
- Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6.The Journal of biological chemistry · 2015Article
- Base-CP proteasome can serve as a platform for stepwise lid formation.Bioscience reports · 2015Article
- Human cytomegalovirus UL76 elicits novel aggresome formation via interaction with S5a of the ubiquitin proteasome system.Journal of virology · 2013Article
- Article
- Negative regulation of 26S proteasome stability via calpain-mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons.The Journal of biological chemistry · 2013Article
- Article
- A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress.Journal of molecular biology · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
An rpn11-1 temperature-sensitive mutant shows defect in proteolysis, mitochondrial function and proteasome assembly. The Rpn11 protein is a proteasome subunit that deubiquitinates proteolytic substrates. Multiubiquitinated proteins interact with proteasome receptors, such as Rpn10, which intriguingly is also required for promoting proteasome stability. We report here that Rpn10 binds Rpn11, and genetic studies revealed synthetic lethality of an rpn11-1 rpn10Δ double mutant. The carboxy-terminus of Rpn11 is critical for function, as deletion of 7 C-terminal residues prevented suppression of rpn11-1 rpn10Δ. Native gel electrophoresis showed increased levels of the proteasome 20S catalytic particle in rpn11-1 rpn10Δ, and altered assembly. The inviability of rpn11-1 rpn10Δ was suppressed by rpn10(uim), a mutant that can bind the proteasome, but not multiubiquitin chains. rpn10(uim) reduced the levels of free 20S, and increased formation of intact proteasomes. In contrast, rpn10(vwa), which binds multiubiquitin chains but not the proteasome, failed to suppress rpn11-1 rpn10Δ. Moreover, high levels of multiubiquitinated proteins were bound to rpn10(vwa), but were not delivered to the proteasome. Based on these findings, we propose that the lethality of rpn11-1 rpn10Δ results primarily from altered proteasome integrity. It is conceivable that Rpn10/Rpn11 interaction couples proteasome assembly to substrate binding.
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