IndraLab

Statements

TP53 binds USP28. 14 / 14
| 2 12
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"Cuella-Martin et al. show that 53BP1 bridges interactions between p53 and the deubiquitinating enzyme USP28, promoting p53-DNA interactions to globally enhance p53-dependent transcriptional programs."
27546791
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"The 53BP1 BRCT Domain Mediates Bivalent Interactions with p53 and USP28."
27546791
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"53BP1 controls p53-dependent responses through direct binding of p53 and USP28 (Cuella-Martin et al., 2016) and promotes NHEJ-mediated DSB repair by inhibiting DNA end resection (Panier and Boulton, 2013; Setiaputra and Durocher, 2019)."
33606978
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"Interestingly, the tandem BRCT domain is known to interact with p53 and USP28 ( xref ; xref ; xref ; xref )."
27371829
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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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"Thus, our data identify an important role for 53BP1-bridged p53-USP28 interaction in regulating p53 function in human cells."
27546791
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"Here, 53BP1’s C-terminal BRCT domains bridge p53’s interaction with the deubiquitinating enzyme USP28, catalysing de-ubiquitination events that stimulate p53 binding to, and activation of, target gene promoters xref ."
30559443
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"This would be consistent with a putative cooperation between p53, 53BP1, and USP28 in tumor suppression."
27546791
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"Furthermore, USP28 and p53 bind the BRCT repeats at different interfaces, and it has been shown that 53BP1 and USP28 share a coregulatory role in supporting p53 functions [20] ( Figure 1 B,C)."
28188027
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"53BP1-dependent p53 modulation requires both auto-oligomerization and tandem-BRCT domain-mediated bivalent interactions with p53 and the ubiquitin-specific protease USP28."
27546791
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"Furthermore, USP28 and p53 bind the BRCT repeats at different interfaces, and it has been shown that 53BP1 and USP28 share a co-regulatory role in supporting p53 functions [ xref ] ( xref )."
28188027
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"This hypothesis is further supported by biochemical work showing that both p53 and USP28 interact with the tandem-BRCT domains of 53BP1 [ xref – xref ], which are dispensable for the DNA damage response role of 53BP1 [ xref ], but are required for the centrosome surveillance pathway [ xref ]."
28188027
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"53BP1 controls p53-dependent responses through direct binding of p53 and USP28 ( xref ) and promotes NHEJ-mediated DSB repair by inhibiting DNA end resection ( xref ; xref )."
33606978
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"This hypothesis is further supported by biochemical work showing that both p53 and USP28 interact with the tandem-BRCT domains of 53BP1 [15–17] , which are dispensable for the DNA damage response rol[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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