RPN11 Antibody

1. Report the ubiquitin-bound structure of Rpn11 from S. cerevisiae and the mechanisms for mechanochemical coupling of substrate degradation and deubiquitination. PMID: 28844860
2. A key role for rpn11 in 26S proteasome PMID: 26182356
3. Fluorescently labeled tetra-Ub chains revealed endo-chain preference for Ubp6 acting on Lys(48) and random action for Rpn11. PMID: 25389291
4. Overall, this work demonstrates that the co-opted Rpn11p, which is involved in the assembly of the functional proteasome, also functions in the proper assembly of the tombusvirus viral replicase complex. PMID: 25540361
5. Rpn11-Rpn8 interaction occurs via two distinct interfaces; Rpn11 lacks a conserved surface to bind the ubiquitin Ile44 patch PMID: 24463465
6. The Rpn11 active site at the entrance to the ATPase ring pore is likely to prevent erroneous deubiquitylation of folded proteins. PMID: 24516147
7. Data show that the availability of Rpn11 is important for maintaining adequate levels of intact proteasomes, as its depletion caused growth and proteolytic defects in rpn3. PMID: 21619884
8. The authors analyzed the rpn11-m1 phenotypes and found that overexpression of Cdc14 suppresses all the rpn11-m1 defects, including the mitochondrial ones. PMID: 21059189
9. It is conceivable that Rpn10/Rpn11 interaction couples proteasome assembly to substrate binding. PMID: 20941496
10. These results suggest that Mpr1-dependent arginine synthesis confers stress tolerance. PMID: 20550582
11. We report that different rpn11 mutations can affect proteasome interaction with ubiquitinated proteins PMID: 20061387
12. The possibility of use of the Saccharomyces cerevisiae MPR1 gene (ScMPR1) encoding the AZC-detoxifying enzyme as a dominant selection marker in Z. rouxii was examined PMID: 17004651
13. Rpn11 controls the mitochondrial shape and show that Rpn11 may regulate the mitochondrial fission and tubulation processes. PMID: 18172023
14. This result suggests that Tyr166 of MPR1 is critical for the catalysis. PMID: 18373682
15. In order to reveal the structural fundamentals of substrate recognition and the catalytic mechanism, X-ray crystallographic studies of Mpr1 have been initiated. PMID: 19194013

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KEGG: sce:YFR004W

STRING: 4932.YFR004W