IndraLab

Statements

DTX3L binds USP28. 7 / 7
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"First, we examined whether the interaction between DTX3L and USP28 would be impaired after DSB induction, but the co-immunoprecipitations showed that this was not the case ( xref A)."
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"These studies on the DTX3L–USP28 interaction suggest synergistic roles in DNA damage repair and cancer biology."
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"All in all, these experiments revealed physical and functional interactions between DTX3L and USP28 assembling Ub E3 ligase and DUB activities, respectively, directed toward both enzyme components of the heterodimeric complex and to downstream proteins involved in signaling different types of stress such as hypoxia or DNA damage."
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"To further investigate the potential direct interaction between DTX3L and USP28, we next employed a proximity ligation immunoassay (PLA) and co-immunoprecipitation analyses."
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"While our findings underscore the essential role of the DTX3L-USP28 feedback loop in cellular homeostasis, the study has limitations."
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"While the co-immunoprecipitation analyses from whole cell lysates verify the interaction of endogenous DTX3L and USP28, the PLA assay revealed fluorescence signals indicating an interaction between USP28 and DTX3L in both, the cytoplasm and in the nucleus ( xref A–1C)."
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"To further investigate the direct USP28-DTX3L interaction and to determine their binding affinity in solution, we next expressed both proteins recombinantly and performed interaction measurements with microscale thermophoresis (MST)."
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