IndraLab
Statements
reach
"The molecular underpinnings of the disassembly of 53BP1–USP28 complexes upon genotoxic stress remain to be investigated but can involve proteasomal degradation of 53BP1 (93) or its recruitment to modified histones at DNA damage sites (3), which could sterically interfere with USP28 binding.In our model, dimerization of USP28 limits unscheduled DNA replication at transcriptionally active loci by preventing ectopic recruitment of PAF1 to MYC."
sparser
"The molecular underpinnings of the disassembly of 53BP1–USP28 complexes upon genotoxic stress remain to be investigated but can involve proteasomal degradation of 53BP1 ( xref ) or its recruitment to modified histones at DNA damage sites ( xref ), which could sterically interfere with USP28 binding."
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
"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)."