IndraLab

Statements

OTUD3 activates YY1. 13 / 13
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"Therefore, we postulated that OTUD3 promotes CRC progression by up-regulating YY1."
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"Overall, these findings are in agreement with our experimental findings on OTUD3-mediated YY1 stability."
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"OTUD3 enhances the stability of YY1 by cleaving ubiquitin molecules from YY1 at K332, K339 and K409 residues."
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"Over-expression of OTUD3 suppressed YY1 degradation and promoted CRC cell growth."
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"Our findings suggest that OTUD3 promotes CRC progression by up-regulating YY1, and provides insights into the underlying mechanisms of YY1 over-expression in CRC."
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"These results suggest that OTUD3 tightly controls YY1 protein stability.Next, we investigated the downstream effects of OTUD3-mediated YY1 regulation."
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"We then investigated how OTUD3 enhances YY1 stability."
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"In summary, OTUD3 enhances YY1 stability by selectively removing K48-linked polyubiquitination chains from the YY1 protein."
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"OTUD3 accelerates CRC progression by up-regulating YY1."
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"Over-expression of OTUD3 significantly increased YY1 protein expression and suppressed its ubiquitination, whereas OTUD3 knockdown or knockout increased YY1 degradation."
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"To determine whether OTUD3 promotes tumor progression by regulating YY1, we restored the expression of YY1 in endogenous OTUD3 depletion CRC cells or knocked down endogenous YY1 in OTUD3-overexpressing CRC cells."
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"Moreover, PLK1 phosphorylates Ser-326 of OTUD3, thereby promoting the binding and stabilization of YY1."
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"Over-expressed OTUD3 inhibited YY1 degradation, thereby increasing YY1 protein levels, whereas OTUD3 knockdown or knockout promoted YY1 degradation, thereby decreasing the proliferation of colorectal cancer (CRC)."
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