IndraLab

Statements


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"Our studies reveal a critical role of OTUD5 in tumorigenesis, as indicated through its interaction with TRIM25, suggesting that the OTUD5-TRIM25 axis acts as an important transcriptional regulator in tumor progression."

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"Taken together, our study sheds light into regulation and function of the OTUD5-TRIM25 axis, suggesting it as a potential target for tumor therapy."

No evidence text available

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"However, some TRIM25 coprecipitated with the Flag-OTUD5-ΔUIM, indicating that the UIM may not be the sole interaction site and that TRIM25 may bind to the other parts of the OTUD5 protein (Fig.  xref )."

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"In addition, the OTUD5/TRIM25 double knockdown cells formed smaller tumor sphere than did the OTUD5-depleted cells, demonstrating that the OTUD5-TRIM25 axis plays an important role in the regulation of tumor growth."

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"To determine the importance of UIM in the interaction between OTUD5 and TRIM25, we transfected Hep3B cells with plasmid constructs expressing Flag-tagged wild-type OTUD5 (Flag-OTUD5-WT) and Flag-tagged OTUD5 with the UIM domain deleted (Flag-OTUD5-ΔUIM) (Fig.  xref )."

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"A significantly lower level of TRIM25 was obtained with Flag-OTUD5-ΔUIM than with Flag-OTUD5-WT, suggesting that the UIM domain is important for the interaction between OTUD5 and TRIM25."

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"The enriched biological processes were dominated by cell cycle and cell division processes, implying that the OTUD5-TRIM25 axis may affect cell proliferation by regulating the cell cycle (Fig.  xref )."

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"We confirmed the interaction between endogenous OTUD5 and TRIM25 by the immunoprecipitation (IP) of Hep3B cells lysates."

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"We tested whether the OTUD5-TRIM25 axis would affect tumor growth in a mouse model."

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"The OTUD5-TRIM25 axis regulates liver cancer development."

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"Further investigation is needed to understand the precise regulatory mechanism underlying the OTUD5-TRIM25 function."

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"OTUD5-TRIM25 transcriptionally regulates the expression of the putative tumor suppressor PML, which is dependent on the intact TRIM25 RING domain."