IndraLab

Statements

USP33 binds TP53. 9 / 9
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"We then examined the association of USP33 with p53 under DNA damage condition."
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"In particular, DNA damage agents can enhance the association of USP33 and p53 resulting in the removal of K48 polyubiquitination on p53 and consequent protein stabilisation."
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"To further verify the interaction between p53 and USP33, 293T whole cell lysates were incubated with control IgG or anti‐USP33 antibody, followed by Western blotting analysis on the pull‐down complex."
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"The result showed that the interaction between USP33 and p53 was substantially enhanced upon cisplatin, CPT or Dox treatment (Figure  xref )."
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"Consistently, the interaction between USP33 and p53 showed a marked enhancement after CPT treatment (Figure  xref )."
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"In an effort to search for the downstream effector of USP33, we found p53 protein level was substantially decreased upon USP33 knockdown, which drives us to explore the association of USP33 and p53 under pathophysiological conditions."
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"We then performed GST‐pulldown assay, and the results confirmed a direct interaction between p53 and USP33 (Figure  xref )."
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"We further determined which domains of p53 interacts with USP33 by constructing different functional domains of Flag‐p53‐N, Flag‐p53‐M and Flag‐p53‐C, and found that both Flag‐p53‐N, Flag‐p53‐M, instead of Flag‐p53‐C, interact with USP33 (Figure  xref )."
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"The findings of USP33 directly interacting with p53 drove us to determine whether USP33 deubiquitinates p53 and further regulates its stability."
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