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PSMD14 binds PSMD7. 40 / 40
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"Here we describe a method for the purification of the Rpn8/Rpn11 heterodimer and ubiquitin-GC-TAMRA, a model substrate that can be used to characterize the DUB activity of Rpn11 in isolation without the need of purifying 26S proteasomes."
36350544
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"After transferring Zn ion to the Rpn11, we used both the Rpn11 monomer (Figure 2A) and the Rpn8-Rpn11 heterodimer (Figure 3A) structures for subsequent analysis.For the CSN5 monomer (Figure 2B), the recently solved crystal structure of CSN5 with CSN5i-3 (PDB_code: 5JOG) (Schlierf et al., 2016) was considered."
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"In the Rpn8-Rpn11 heterodimer, capzimin showed a bidentate coordination with Zn and a stable H-bond with side chain of Thr129 (Figure S4B)."
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"This feature opens the possibility that the regulatory particle, free lid subcomplex or the heterodimer PSMD14-PSMD7 might play other physiological roles including a positive function on protein stability through deubiquitination."
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"Thus, we investigated whether this was an unrealistic over binding, a protein-protein complex environment would be able to reproduce the selectivity.In the heterodimeric Rpn8-Rpn11 complex, CSN5i-3 binding in the pocket was not stable (Figure 7C), the distance to zinc increases continously and eventually the ligand lost coordination with Zn (Figure 7D and Table 1) which shows that the influence of Rpn8 on the capzimin bound Rpn11 is prominent."
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"PSMD7 interacts with PSMD14 to activate proteasome function to regulate ubiquitinated substrate degradation."
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"Finally, we discuss why this information should be investigated in biomedicine specifically with focus on cancer progression to design new therapeutic strategies against the lid subcomplex and the heterodimer PSMD14-PSMD7, highlighting PSMD14 as a druggable target for cancer therapy."
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"PSMD14 and Rpn11 forms a dimer with PSMD7 and Rpn8 and catalyzes deubiquitylation."
25943340
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"We propose that disruption of the PSMD7 and PSMD14 complex may block p53 degradation in the proteasome and therefore trigger cell cycle arrest, senescence and apoptosis in LUAD cells."
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"Both crystal structures of the yeast Rpn8-Rpn11 heterodimer (Pathare et al., 2014) and the cryo-EM structure of human 26S proteasome (Huang et al., 2016) show that the α2 helices of both proteins makes extensive contacts with each other.Molecular dynamics simulations refined the binding position of capzimin."
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"The final Rpn8-Rpn11 heterodimer model is shown is Figure 3A and Figure S1C."
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"Disruption of PSMD14 and PSMD7 heterodimers may affect p53 degradation in the proteasome."
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"Research on the proteasome holoenzyme revealed that PSMD14 and PSMD7 can form a dimer, which is locating directly above the central pore and leading the degraded substrate enter into the N‐terminal‐domain ring of the base ATPases xref ."
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"Research on the proteasome holoenzyme revealed that PSMD14 and PSMD7 can form a dimer, which is locating directly above the central pore and leading the degraded substrate enter into the N-terminal-domain ring of the base ATPases 13."
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"In the case of the Rpn8-Rpn11 heterodimer, LIE calculations showed only a very low binding energy of CSN5i-3 (Table 2) which is in agreement with the reported ligand binding selectivity."
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"However in the case of the Rpn8-Rpn11 heterodimer, CSN5i-3 showed only very weak interaction."
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"We propose that disruption of the PSMD7 and PSMD14 complex may block p53 degradation in the proteasome and therefore trigger cell cycle arrest, senescence and apoptosis in LUAD cells."
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"27 Å in Rpn11 monomer and Rpn8-Rpn11 heterodimer, respectively."
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"LIE calculations (Table 2) revealed that CSN5i-3 binds moderately to the monomeric Rpn11 and very weakly to the Rpn8-Rpn11 heterodimer."
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"Binding of capzimin and CSN5i-3 to monomeric Rpn11 and Rpn8-Rpn11 heterodimer."
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"The third DEP, PSMD7 (Rpn8), is part of the Rpn8-Rpn11 heterodimer with a function in removal of polyubiquitin tags before protein degradation in the proteasome 30 ."
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"Proteasome 26S subunit, non-ATPase 7 (PSMD7, Rpn8, Mov34), an ATP-independent component of the 19S regulatory subunit, forms the heterodimers with PSMD14 as a functional complex which is extremely critical for degradation of ubiquitinated substrate with the proteasome [ xref ]."
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"The starting structures of CSN5i-3 bound to the monomeric Rpn11 and Rpn8-Rpn11 heterodimer were generated by manual docking."
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"Disruption of PSMD14 and PSMD7 heterodimers may affect p53 degradation in the proteasome."
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"PSMD7 interacts with PSMD14 to activate proteasome function to regulate ubiquitinated substrate degradation."
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"Capzimin showed almost similar binding affinity to monomeric Rpn11 as well as Rpn8-Rpn11 heterodimer (Table 2)."
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"A proteasomal subunit in close proximity to the Rpn8-Rpn11 heterodimer is PSMD13 (Rpn9), which showed a trend towards upregulation (fold change = 4.2; p = 0.07)."
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