IndraLab

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USP14 inhibits proteolysis. 28 / 29
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"In contrast, RNAi of either UCHL5 or USP14 alone did not affect cell growth, proteasome structure, or proteolytic capacity, but increased the rate of protein degradation."
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"USP14 reduces proteolysis in a substrate-specific manner by rapidly trimming the tagging ubiquitin chains before the 26S proteasome can initiate degradation of that substrate [ 350 ] ."
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"In contrast, RNAi of Uch37 or Usp14 had no detectable effect on cell growth, proteasome structure or proteolytic capacity, but accelerated cellular protein degradation."
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"USP14 was found to promote the UPS-mediated K48-ubiquitinated AR protein degradation."
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"The RNAi of UCHL5 or USP14 alone does not affect cell growth and proteasome composition but accelerates cellular protein degradation; however, RNAi of both UCHL5 and USP14 can inhibit cellular protein degradation."
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"RNAi of either Uch37 or USP14 (the mammalian homologue of yeast Ubp6) accelerates protein degradation."
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"Small molecule inhibitor of USP14, IU1, enhances proteasomal proteolysis of ubiquitinated substrate in T cells obtained from young but not those from elderly donors."
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"The deubiquitinating enzyme Usp14 allosterically inhibits multiple proteasomal activities and ubiquitin independent proteolysis."
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"USP14 prevents protein substrate degradation by blocking the ubiquitin chain and promoting protein degradation by activating proteases (Wang F. et al., 2021)."
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"USP14 regulates proteasome activity and pharmacologic inhibition of USP14 increases the rate of protein degradation in the cell XREF_BIBR."
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"It was reported that AKT-mediated phosphorylation of USP14 at Ser432 activated its deubiquitinating activity for both K48 and K63 ubiquitin linkages, thus regulating protease activity and consequently[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"For example, USP14, known to inhibit protein degradation via the UPS by cleaving the K48-linked ubiquitin chain from the target, could also modulate the autophagy by promoting the K63-linked deubiquitination of specific targets, such as Beclin1."
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"Importantly, whereas knockdown of POH1 interferes with the proteasome assembly, depletion of either USP14 or UCH37 alone does not affect or even slightly enhances protein degradation rates."
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"A study conducted in 2010 showed that USP14 inhibits protein degradation by the proteasome in murine embryonic fibroblasts."
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"UBL domain of Usp14 and other proteins stimulates proteasome activities and protein degradation in cells."
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"We also identified the putative ubiquitination residues in PER through mass spectrometry and found that mutations in the lysine residue to alanine at positions 1117 and 1118 rendered the protein resistant to USP14-mediated protein degradation."
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"Since the loss of USP14 accelerates cellular proteolysis, we performed a quantitative proteomic analysis to determine the levels of proteins in WT H4 cells, H4 USP14-KO cells, and H4 USP14-KO cells complemented with WT USP14, S143A and S432A (AA), or S143D and S432D (DD) mutants."
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"These studies further confirmed two observations noted independently, i.e., (1) that inhibition of USP14 up-regulates proteasomal proteolysis in the cells from young donors, perhaps by virtue of 20S gate opening, but fail to do so in cells from the elderly, and (2) that inhibition of USP14 in T cells from both young and elderly donors influences the levels of poly-ubiquitinated proteins and free ubiquitin."
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"Thus, the presence of Usp14 on the 26S helps reduce wasteful ATP consumption and nonselective proteolysis."
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"Interestingly, b-AP15, a dual inhibitor of Usp14 and Uch37, was shown to prevent protein degradation and inhibit tumor progression in acute myeloid leukemia models [222]."
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"Although present in Xenopus extracts (N.V.D., R.W.K., unpublished data), levels of USP14 associated with proteasomes in extract may be insufficient to impede proteolysis."
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"The deubiquitinating enzyme Usp14 allosterically inhibits multiple proteasomal activities and ubiquitin independent proteolysis."
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"Double knockdown of Ubp6/USP14 and Uch37/UCHL5 results in inhibition of cell growth, decreased protein degradation, and accumulation of polyubiquitinated proteins, a phenotype similar to that observed[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Knockdown of USP2 or USP14 accelerated protein degradation of TNF-alpha, and abolished the effect of miR-124 on TNF-alpha protein stability."
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"USP14 , one member of the ubiquitin-specific proteases DUBs family , is associated with the proteasome complex and inhibits proteolysis by catalyzing protein deubiquitination ( 14 ) ."
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"Mouse embryonic fibroblasts lacking USP14 show enhanced clearance of several disease related proteins, including tau and polyglutamine expanded ataxin-3, and overexpression of catalytically inactive USP14 increases protein degradation [XREF_BIBR]."
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"Conversely, in the absence of substrate, binding of the UBL domain of USP14 or Ubp6 to the regulatory particle leads to the suppression of the proteasomal activity, delaying protein degradation."
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"Theoretically, a true proteolysis associated substrate of USP14 will be degraded by USP14 KD through its elevated protein ubiquitination level, and will interact with USP14."
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