IndraLab

Statements


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"To confirm this, we tested TRIM11 on recombinant USP14 protein that were activated by proteasome enriched cell lysates or purified RPs."

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"The 26S proteasome-activated USP14 is capable of cleaving single ubiquitin from its substrates and removing the en-bloc ubiquitin chains from substrates ubiquitinated at multiple sites, until only a single chain remains (Lee et al., 2016)."

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"This is consistent with previous studies showing that PGJ2 lowers 26S proteasome levels and activity [XREF_BIBR, XREF_BIBR], and inhibits some of the thiol deubiquitinases including UCH-L1 and UCH-L3 [XREF_BIBR, XREF_BIBR], as well as Ub-isopeptidase activity [XREF_BIBR], but not USP14 as shown here in our current studies."

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"Based on the structure of USP14, several inhibitors with high potency and selectivity, such as IU1 and IU1 derivatives, have been discovered and characterized for their ability to inhibit 26S proteasome-activated USP14 in an allosteric manner at both cellular and in vivo levels."

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"XREF_FIG shows that free chains of diverse length and linkage type are all cleaved minimally by proteasome activated USP14, even upon long incubation."

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"Again, this proteasome mediated USP14 activation was effectively prevented by recombinant TRIM11."

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"Still, USP14 activity can be remarkably enhanced by association with the proteasome -- up to ~ 800-fold -- suggesting its major regulatory role in proteasome function [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

sparser
"This suggests that a unique negative feedback model, in which USP14 is activated by proteasome and then proteasomal degradation is suppressed by deubiquitination, is the basis by which USP14 serves as a critical inhibitory component of the proteasome [ xref , xref , xref ]."

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"Indeed, phosphorylation of Usp14 (or the use of a Usp14 phosphomimetic) results in increased activity in assays with the fluorogenic substrate ubiquitin-7-amino-4-methylcoumarin (Ub-AMC), for both Usp[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"The resolution of this conundrum required the identification of a preferred substrate of Usp14 and of the properties that govern substrate preference.Cyclin B, ubiquitinated by its physiological ligas[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"This suggests that a unique negative feedback model, in which USP14 is activated by proteasome and then proteasomal degradation is suppressed by deubiquitination, is the basis by which USP14 serves as a critical inhibitory component of the proteasome [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

sparser
"These results indicate that USP14 aptamer-induced proteasome activation might protect cells under various stressful conditions, including neurodegeneration."

sparser
"It is different from the mechanism by which the proteasome activates USP14."

sparser
"Based on the structure of USP14, several inhibitors with high potency and selectivity, such as IU1 and IU1 derivatives, have been discovered and characterized for their ability to inhibit 26S proteasome-activated USP14 in an allosteric manner at both cellular and in vivo levels."

sparser
"The 26S proteasome-activated USP14 is capable of cleaving single ubiquitin from its substrates and removing the en-bloc ubiquitin chains from substrates ubiquitinated at multiple sites, until only a single chain remains ( xref )."