IndraLab
Statements
Proteasome activates USP14. 15 / 16
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10
5
reach
"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."
reach
"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
"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."