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UCHL5 binds RPN13. 32 / 32
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"These results were compared with the oligomerization state and stoichiometry of the Uch37 and Rpn13 complex in solution to determine whether a change in the oligomerization state of the protein results in the activation of Uch37."
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"Therefore, we used this Rpn13C for further analysis of the Rpn13 and Uch37 complex."
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"In vitro binding of Uch37 with Rpn13 was shown to promote the hydrolysis of ubiquitin-7-amido-4-methylcoumarin (Ub-AMC) and Uch37 's reactivity with suicide inhibitors such as ubiquitin vinylsulfone (UbVS) and ubiquitin aldehyde (Ubal)."
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"However, this modification did not restore the same degree of activity that was achieved by the Rpn13 and Uch37 complex."
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"Furthermore, we discovered that IkappaB-alpha, a protein whose proteasomal degradation activates the transcription factor NF-kappaB, is also a substrate for the Rpn13 and UCH37 complex."
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"Ubiquitin receptors play an integral role in substrate capture and apparently contribute to ubiquitin chain deconjugation, as Rpn13 binds and activates deubiquitinating enzyme Uch37."
19683493
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"Usp14 (yeast UBP6) is associated with Rpn1 21) and Uch37 binds to the C-terminal domain of Rpn2 bound Rpn13; i.e., Uch37 associates with the base via Rpn13."
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"The binding of Rpn13 to the KEKE motif of Uch37 likely perturbs the hydrophobic interactions of tetrameric Hc, resulting in disassembly of the oligomer into a monomer via the formation of a stable Rpn13 and Uch37 complex that provides a means to keep Uch37 in the monomeric state."
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"Rpn13 also binds and activates deubiquitinating enzyme Uch37, one of the proteasome 's three deubiquitinating enzymes."
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"While the UCH-L5 and RPN13 complex is equimolar at 1:1, the ligand number in our ITC analysis (between 0.25 and 0.5) suggests that the BAP1 and ASXL1 DEU complex is asymmetric and consists of multiple BAP1 molecules bound to one ASXL1 DEU molecule."
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"Because of a previous discovery of an interaction between Rpn13 and inducible nitric oxide synthase (iNOS), we hypothesized that iNOS is one of the substrates for the Rpn13 and UCH37 complex."
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"Rpn13 also binds to the Uch37 and UCHL5 deubiquitylating enzyme via its carboxy-terminal domain, called the deubiquitinase adapter (DEUBAD) domain."
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"The UCH37 and Rpn13 interaction is dependent on a short KEKE-motif within the ULD of UCH37 [XREF_BIBR]."
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"In fact, crystal structures of a ternary complex of UCHL5 bound to Rpn13 and ubiquitin XREF_BIBR, XREF_BIBR revealed that a segment of the crossover loop (Met148 and Phe149) interacts directly with Rpn13, while the rest remains disordered (XREF_FIG)."
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"The structure was solved by molecular replacement with the programme Phaser-MR 51 using the coordinates of the UCH-L5 and RPN13 complex (PDB code : 4UEM) 16 as a search model."
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"As with the case of Uch37 binding to Rpn13, Ubp6 is activated by association with Rpn1, and Ubp6 also seems to modify 19S RP structure because its binding delays proteolysis by a mechanism that is independent of its catalytic activity."
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"Recruitment to the proteasome is mediated by RPN13 (also known as ADRM1), whose C-terminal domain (RPN13 CTD) binds the UCH37 CTD and greatly stimulates activity against model substrates, whereas the RPN13 N-terminal domain binds the large proteasome scaffolding subunit RPN2."
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"We demonstrate that the enzymatic activity is mechanistically similar to the related UCH-L5 and RPN13 complex."
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"Binding of Rpn13 to Uch37 increases the isopeptidase activity of Uch37; therefore it may facilitate the rescue of ubiquitinated substrates from proteolysis XREF_BIBR, XREF_BIBR, XREF_BIBR."
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"A recent publication has provided further proof of the selective role of Rpn13 in proteasomal function by identifying nitric oxide synthase and IkappaB-alpha as two specific substrates of the Rpn13 and Uch37 complex XREF_BIBR."
21048919
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"RPN13 presumably interacts with the ubiquitin carboxyl-terminal hydrolase UCH-L5 and UCH37 (## 20, 21 in Fig. 2 A) [34,35]."
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"Recent studies reveal that mechanism of H2A deubiquitination by BAP1-ASXL1 in PR and DUB complex is similar to UCHL5 and RPN13 complex [XREF_BIBR, XREF_BIBR] where DEUBiquitinase ADaptor domain (DEUBAD) [XREF_BIBR] of ASXL1 interacts with ULD of BAP1 and increases the affinity of BAP1 for ubiquitin [XREF_BIBR, XREF_BIBR]."
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"Rpn13 binds the carboxy-terminal tail of UCHL5 in order to recruit it into proteasome through binding to Rpn2 subunit of the 19S complex [XREF_BIBR - XREF_BIBR]."
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"In contrast to a previous report, we find that RPN13 binds ubiquitin with an affinity similar to that of other proteasome associated ubiquitin receptors and that RPN2, ubiquitin, and the deubiquitylase UCH37 bind to RPN13 with independent energetics."
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"While the UCH-L5 and Rpn13 complex has provided a template for PR-DUB catalysis and modelling of some cancer derived mutations XREF_BIBR, XREF_BIBR, XREF_BIBR, many outstanding questions remain unanswered."
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"The specific substrates for the Rpn13 and UCH37 complex have not been determined."
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"The 1:1 topology is similar to that observed for the related deubiquitinase UCH-L5 bound to its proteasomal activator Rpn13."
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"To understand the mode of auto-inhibition clearly and shed light on the activation mechanism of Uch37 by Rpn13, we investigated the Uch37 and Rpn13 complex using a combination of mutagenesis, biochemical, NMR, and small-angle X-ray scattering (SAXS) techniques."
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"We also demonstrated that Rpn13C (Rpn13 residues 270-407) could disrupt the oligomerization of Uch37 by sequestering Uch37 and forming a Uch37 and Rpn13 complex."
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"Rpn13 can interact with Uch37 and recruit it to the proteasome via its C-terminal 46 residues (also called the KEKE motif) and activates Uch37."
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"Furthermore, whereas the Rpn13 and Uch37 complex can hydrolyze only small adducts of ubiquitin, such as Ub-AMC, a Rpn13 and Uch37 complex that is incorporated on 19S RP can process large ubiquitin conjugates, such as di-ubiquitin."
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"To gain a clear understanding of the auto-inhibition mechanism of Uch37 and the Uch37 activation by Rpn13, we investigated the Uch37 and Rpn13 complex using a combination of mutagenesis, biochemical, NMR, and SAXS analyses."
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