IndraLab

Statements


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sparser
"Furthermore, a 53BP1-USP28 complex was identified as an activator of p53-mediated transactivation ( xref , xref , xref , xref )."

sparser
"In particular, the TTD residues V1544 and G1560, located opposite to the methyl-K/R binding pocket ( xref ) ( xref ), define a non-canonical TTD interaction surface that promotes the association of 53BP1 with USP28."

sparser
"Different from the interaction of USP28 with LSD1, USP28-mediated p53BP1 stabilization only occurs after DNA damage and no effect is found in the absence of DNA damage, suggesting that the interaction between USP28 with p53BP1 is regulated by DNA damaging."

reach
"Furthermore, a 53BP1-USP28 complex was identified as an activator of p53-mediated transactivation (Cuella-Martin et al., 2016a, Fong et al., 2016, Lambrus et al., 2016, Meitinger et al., 2016)."

sparser
"Here, we describe the TTD as the second 53BP1 domain, in addition to the tandem BRCT, that regulates the USP2853BP1 interaction ( xref ) ( xref ; xref )."

reach
"While much remains to be learned about how the mitotic surveillance pathway functions to survey centrosomes, a plausible model is that in response to centrosome loss, 53BP1 binds to USP28 and p53 to facilitate USP28 dependent deubiquitination and activation of p53, leading to cell cycle arrest XREF_BIBR, XREF_BIBR (XREF_FIG)."

reach
"Taken together, a body of evidence supports a model in which a 53BP1 and USP28 complex modulates p53 activity in response to centrosome loss."

No evidence text available

reach
"For example, the DNA damage response pathway is central to the maintenance of genomic stability and both members of a key DDR complex, the TP53BP1 and USP28 complex, which are substrates of the ATM kinase, were identified within the top 110 TSGs (q-value < 0.15, XREF_FIG, XREF_FIG)."

sparser
"USP28 has been reported to regulate TP53 abundance in a USP28-TP53BP1 cell cycle-dependent fashion [ xref – xref ]."

sparser
"Thus, consistent with the known interaction of 53BP1 with USP28, we show that while 53BP1 has no deubiquitinase activity, it can function upstream of USP28 to stabilize p53."

No evidence text available

sparser
"We found that 53BP1 binding to USP28 was specifically attenuated by the R1811A BRCT mutation, yet unaffected by the K1814M phospho-binding or p53-binding mutations ( xref D)."

No evidence text available

reach
"Important future directions include dissecting the interactions between 53BP1 and USP28 that activate downstream p53-p21 signaling, as well as screening for the upstream components that transduce the signal (see Outstanding Questions)."

sparser
"It was previously reported that USP28 is involved in the regulation of TP53 protein abundance in a USP28TP53BP1 cell cycle‐dependent fashion (Fong et al , xref ; Lambrus et al , xref ; Meitinger et al , xref )."

sparser
"Interaction with ATM contributes to the binding of USP28 to TP53BP1, the overall role of USP28 in DNA damage signaling, however, was unclear [ xref ]."

reach
"The cooperation between 53BP1 and USP28 in triggering p53 dependent growth arrest following N3 treatments prompted us to investigate their function in arresting the cell cycle in response to DNA damage."

reach
"We found that 53BP1 binding to USP28 was specifically attenuated by the R1811A BRCT mutation, yet unaffected by the K1814M phospho binding or p53 binding mutations (XREF_FIG D)."

reach
"USP28 and p53 both bind to 53BP1 through the tandem C-terminal BRCT repeats."

reach
"This would be consistent with a putative cooperation between p53, 53BP1, and USP28 in tumor suppression."

No evidence text available

reach
"Taken together, a body of evidence supports a model in which a 53BP1 and USP28 complex modulates p53 activity in response to centrosome loss.While little is known about the upstream mechanism of ' sen[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Remarkably, the interaction between 53BP1 and USP28 was completely abolished by the G1560K mutation and largely diminished by the V1544I mutation, while the G1593K mutation increased 53BP1 binding to USP28, thus acting as a GOF mutation (Figure 3F)."

No evidence text available

reach
"Moreover, USP28 binds checkpoint proteins 53BP1, Claspin, and Mdc1 [XREF_BIBR]."

sparser
"Remarkably, the interaction between 53BP1 and USP28 was completely abolished by the G1560K mutation and largely diminished by the V1544I mutation, while the G1593K mutation increased 53BP1 binding to USP28, thus acting as a GOF mutation ( xref )."

No evidence text available