IndraLab

Statements

USP28 deubiquitinates TP53. 8 / 8
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"While 53BP1, USP28, and p53 have not yet been demonstrated to form a ternary complex, USP28 was able to deubiquitinate p53 in vitro [9]."
28188027
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"The signalling pathway involves 53BP1 and the deubiquitylase USP28 acting in a complex to deubiquitylate and stabilise p53, which in turn controls cell fate."
28900014
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"Because 53BP1 is known to bind USP28 as well as p53, a possible scenario is that it bridges the two proteins so that USP28 can deubiquitinate p53, preventing the tumor suppressor from being targeted to the proteasome for degradation."
| PMC
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"However, it was not clear whether USP28 deubiquitinates p53 to stabilize it or regulates its DNA binding function, or whether its impact on p53 is indirect, via other factors."
33961797
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"While 53BP1, USP28, and p53 have not yet been demonstrated to form a ternary complex, USP28 was able to deubiquitinate p53 in vitro [XREF_BIBR]."
28188027
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"The nuclear p53 accumulation caused by overexpression of wild type USP28 was not due to a specific increase in p53 mRNA levels (XREF_FIG), further supporting our observation that USP28 deubiquitinates p53 for protein stabilization."
27371829
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"its interacting protein USP28 that can directly deubiquitinate p53 in vitro and ectopically stabilize p53 in vivo"
27371829
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"Intriguingly, 53BP1 mediates p53 activation independently of its DNA repair activity, but requiring its interacting protein USP28 that can directly deubiquitinate p53 in vitro and ectopically stabilize p53 in vivo."
27371829