IndraLab

Statements

NFRKB inhibits UCHL5. 13 / 16
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"In contrast, NFRKB inhibits UCH37 by blocking the ubiquitin-binding site and by disrupting the enzyme active site."
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"Uch37 activity can be inhibited by NFRKB alone or by incorporation into hINO80."
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"Mechanism of UCH-L5 Inhibition by INO80G DEU ."
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"Interestingly, UCHL5 is activated by the proteasome subunit RPN13 and inhibited by the INO80G subunit ."
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"By contrast, UCH37 is inhibited by the chromatin remodeling complex component INO80G mediated by the N-terminal domain of NFRKB (nuclear factor related to kappaB, NFRKB)."
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"The deubiquitinating enzyme UCH-L5 can be inhibited and activated by regulatory proteins INO80G and RPN13, respectively."
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"Our binding assays showed that INO80G DEU decreases the affinity of UCH-L5 for substrates (XREF_FIG A and 2B)."
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"The related DEUBAD domain in INO80G inhibits UCH-L5 by exploiting similar structural elements in UCH-L5 to promote a radically different conformation, and employs molecular mimicry to block ubiquitin docking."
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"NFRKB NTD inhibits UCH37 because of two distinct contacts that it makes with the UCH domain."
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"Surprisingly, the truncated protein INO80G DEU Deltaalpha6 still inhibited UCH-L5 (XREF_FIG B), demonstrating that helix alpha6 is not required for inhibition under these conditions."
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"Analysis of the UCH-L5 and INO80G DEU interface shows how the large conformational changes in UCH-L5 organize novel interfaces where key elements for ubiquitin binding and RPN13 DEU -mediated activation are exploited by INO80G DEU to inhibit UCH-L5 activity."
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"Inhibition of UCH37 by NFRKB NTD."
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"Interestingly, while UCH37 is inhibited by INO80G, this DUB is activated by RPN13 ."
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