IndraLab

Statements

RPN13 activates UCHL5. 25 / 25
| 25
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"Stimulation of deubiquitylating activity can now be added to this list of proteasomal functions, but neither ATPase nor proteolytic function of the proteasome is required, as Rpn13 alone can activate Uch37."
18922460
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"In line with previous data, we found that the DEUBAD domain of RPN13 activates UCH-L5 (UR)."
25702870
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"Therefore, it appears that Rpn13 can transiently activate Uch37 in a " hit-and-run " manner without disrupting its association with INO80."
18922460
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"We show how the DEUBAD domain in RPN13 activates UCH-L5 by tuning the conformation of structural elements in UCH-L5, and inhibits in INO80G, where it exploits molecular mimicry and UCH-L5 conformational plasticity to prevent ubiquitin docking and catalysis."
25702870
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"That Uch37 binds and is activated by Rpn13 raises the potential for its selective activity on substrates docked via Rpn13."
23672618
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"Rpn13, the proteasomal receptor for Uch37 in the proteasome 19S regulatory particle, can activate UCH37 by disrupting dimerization."
32257396
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"Interestingly, a recent study has shown that the proteasomal subunit RPN13 acts as an accessory protein to enhance the activity of the DUB UCH37 toward K48 containing, branched triubiquitin, and this could provide new ways to further explore the assembly and disassembly of these more complex ubiquitin chain types."
| PMC
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"Mechanism of the Rpn13 induced activation of Uch37."
24752541
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"The DEUBAD Domain of RPN13 Activates UCH-L5 by ULD and CL Positioning."
25702870
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"In this context, the Rpn13 dependent activation of the UCH37 deubiquitinase is noteworthy (cf. XREF_FIG) XREF_BIBR XREF_BIBR, since it would provide SGTA bound substrates with an opportunity for selective deubiquitination XREF_BIBR."
27827410
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"There are likely other factors that contribute to the activation of Uch37 by Rpn13."
24752541
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"The findings help to understand the mechanism of Uch37 auto-inhibition clearly and shed light on the activation of Uch37 by Rpn13."
24752541
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"These observations do not preclude the possibility that Rpn13 enhances Uch37 activity."
21953935
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"Here we show how the DEUBAD domain in RPN13 activates UCH-L5 by positioning its C-terminal ULD domain and crossover loop to promote substrate binding and catalysis."
25702870
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"As discussed below, the differences in UCH domain contacts and the attendant orientations of the CTD helices explain the activation of UCH37 by RPN13 and its inhibition by NFRKB."
25702872
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"RPN13 can activate UCH37 by disrupting dimerization, although physiologically-relevant activation likely results from stabilization of a surface competent for ubiquitin binding and modulation of the active-site crossover loop."
25702872
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"Rpn13 activated Uch37 by forming a 1:1 stoichiometric complex in which the active site of Uch37 was accessible to Ub."
24752541
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"However, the mechanism by which Rpn13 activates Uch37 is not known."
24752541
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"The RNA aptamers significantly delayed RPN13 mediated UCH37 activation and lowered total DUB activity of proteasomes, as measured by the hydrolysis of ubiquitin-rhodamine110."
27930845
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"A mechanism for the activation of Uch37 by Rpn13 is discussed."
24752541
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"Our data show how UCH-L5 activity can be modulated by DEUBAD domains present in RPN13 and INO80G through remarkably large conformational changes."
25702870
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"This result is consistent with the inference derived from the biophysical characterization of the Uch37 and Rpn13C complex that Rpn13 activates Uch37 through its interaction with the C-terminal domain of Uch37, particularly the KEKE motif."
24752541
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"Similarly, UCH37, the human homolog of S. pombe Uch2, is activated by Rpn13, another proteasomal base subunit XREF_BIBR - XREF_BIBR."
20838651
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"The C-terminus of Rpn13 has been shown to specifically bind to and activate Uch37."
24752541
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"Invitro, RPN13 is able to directly promote UCH-L5 activity against a minimal substrate."
25702870