IndraLab

Statements


USP7 increases the amount of FOXP3. 13 / 13
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"USP7 knockdown treatment reduced the expression of endogenous FOXP3 protein, and decreased Tregs cell-mediated inhibition in vitro (70)."

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"On the contrary, USP7 expression decreased polyubiquitination of Foxp3 and enhanced Foxp3 expression (30)."

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"These authors have also shown that the overexpression of USP7 in Tregs increases Foxp3 protein levels (40)."

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"On the contrary, USP7 knockdown in Treg cells promotes Foxp3 polyubiquitination, decreases Foxp3 protein expression, and abrogates Treg-cell-mediated suppressive function in vitro."

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"USP7 is upregulated in Treg cells, and the ectopic expression of USP7 decreases Foxp3 polyubiquitylation and increases Foxp3 expression."

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"USP7 inhibition also decreases levels of FOXP3, a protein required for regulatory T cell (Treg) function."

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"Ectopic expression of USP7 decreases the polyubiquitination of Foxp3 and increases the expression level of Foxp3 protein."

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"In contrast, expression of the deubiquitinase (DUB) USP7 in Treg increased their Foxp3 expression and suppressive function [ 79 ]."

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"The knockdown of USP7 decreased the levels of endogenous FOXP3 and diminished the Treg suppressive activity while ectopic expression of USP7 increased FOXP3 expression by preventing its degradation."

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"Conversely, USP7 knockdown decreases FOXP3 protein levels and abrogates Treg cell-mediated suppression in vitro and in vivo [29] ."

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"These data demonstrate that USP7-mediated de-ubiquitination of FOXP3 can regulate FOXP3 protein levels and thus Treg cell-mediated suppression in vitro ."

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"Our present findings suggest that targeting factors such as USP44 and USP7 that promote FOXP3 expression at the protein level is a strategy that offers exciting possibilities for the fine tuning of immune responses in cancer."

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"Ectopic expression of USP7 decreased FOXP3 polyubiquitination and increased FOXP3 expression."