IndraLab

Statements

DNPEP binds USP4. 13 / 14
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"Mechanistically, FBXO3 disrupts the interaction between USP4 and aspartyl aminopeptidase (DNPEP), thereby protecting USP4 from DNPEP-mediated degradation."
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"FBXO3 binds to USP4 and disrupts the interaction between USP4 and DNPEP, leading to stabilization of USP4 and Twist1."
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"FBXO3 binds to USP4 and disrupts the interaction between USP4 and DNPEP, leading to stabilization of USP4 and Twist1."
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"It has been reported that aspartyl aminopeptidase (DNPEP) can bind to and degrade USP4 [ xref ]."
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"Thus, we suspected that FBXO3 may act to block DNPEP interaction with USP4."
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"Furthermore, knockdown of FBXO3-induced down-regulation of USP4 could not be rescued by either lysosome inhibitor (chloroquine) or proteasome inhibitor (MG132) (Fig 4A and 4B), suggesting that knockdown of FBXO3-induced down-regulation of USP4 is unlikely to be at the transcriptional levels or at the levels of the proteasome-/lysosome-mediated protein stability.It has been reported that aspartyl aminopeptidase (DNPEP) can bind to and degrade USP4 [38]."
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"Importantly, the elevation of FBXO3 expression significantly reduced complex formation between USP4 and DNPEP, whereas silencing of FBXO3 increased endogenous DNPEP binding to USP4 in MDA-MB-231 cells ( xref )."
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"Together, these results indicate that FBXO3 binds USP4 to interfere with the interaction between USP4 and DNPEP, leading to stabilization of the USP4 protein."
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"Notably, aspartyl aminopeptidase (DNPEP) can bind to, hydrolyze, and destabilize USP4 [38]."
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"Importantly, the elevation of FBXO3 expression significantly reduced complex formation between USP4 and DNPEP, whereas silencing of FBXO3 increased endogenous DNPEP binding to USP4 in MDA-MB-231 cells (Fig 4H and 4I)."
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"Together, these results indicate that FBXO3 binds USP4 to interfere with the interaction between USP4 and DNPEP, leading to stabilization of the USP4 protein."
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"Furthermore, while p110α had little effect on DNPEP expression, it significantly up-regulated and prolonged the half-life of FBXO3, leading to disruption of USP4 and DNPEP complex formation (Figs 5C–5E and S4E)."
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"Mechanistically, we found that the ApaG domain of FBXO3 binds to USP4 to prevent USP4 interaction with DNPEP thereby leading to USP4 protein stabilization."
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