IndraLab

Statements

NFRKB activates UCHL5. 8 / 8
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"While the DEUBAD domain of RPN13 activates UCH-L5 by increasing its affinity for substrates, in INO80G it does the opposite and dramatically decreases the affinity for substrates."
26073511
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"To determine whether NFRKB also modulates Uch37 activity, we affinity purified from insect cells recombinant Uch37 in complexes with NFRKB, various NFRKB derivatives, or hRpn13 (XREF_SUPPLEMENTARY) and assayed Uch37 for its ability to react with ubiquitin vinylsulfone (UbVS)."
18922472
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"Why does NFRKB DEU fail to activate Uch37?"
28988953
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"Our observations are consistent with the findings that RPN13 competes with NFRKB 1-101 for binding to UCH37 and that NFRKB residues 1-101 activate UCH37 but that the longer full-length and 1-465 constructs inhibit UCH37, as do the 39-156 and 1-117 constructs used in this study."
25702872
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"Enzyme kinetics analysis confirmed that INO80G short activates UCH-L5 on Ub-AMC (XREF_FIG B)."
25702870
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"INO80G short, containing only the helices alpha2-alpha4 of the DEUBAD domain, can activate UCH-L5, demonstrating that the core DEUBAD fold is already sufficient to bind and provide modest activation."
25702870
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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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"Intriguingly, an artificial shorter version of INO80G was found to activate UCH-L5 invitro."
25702870