IndraLab

Statements


| 9

sparser
"To determine whether V1544, G1560 and/or G1593 regulate the interaction of 53BP1 with p53 and/or USP28, we immunoprecipitated HA-tagged 53BP1 WT and mutant protein complexes from HEK293T cells ( xref )."

sparser
"USP28 and p53 both bind to 53BP1 through the tandem C-terminal BRCT repeats ( xref ; xref )."

sparser
"In line with our transcriptomic analyses ( xref ), our data collectively reveal a function for 53BP1-dependent bivalent interactions with USP28 and p53 in enhancing p53-promoter element interactions, thereby amplifying p53-dependent transcriptional programs."

sparser
"Previous work has shown that both p53 and USP28 directly interact with 53BP1 through its BRCT domains [14,19] ."

sparser
"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 , xref ( xref )."

sparser
"Previous work has shown that both p53 and USP28 directly interact with 53BP1 through its BRCT domains [ xref , xref ]."

sparser
"We therefore hypothesize that 53BP1-USP28 complexes interact with nucleoplasmic p53 pools, where they function to prime p53 DNA-binding activity."

sparser
"Strikingly, unlike unstressedp21 -/- cells that mostly lacked nuclear p53, in the stressed condition, p53 not only was stabilized in the nucleus, but also formed bright nuclear foci of various sizes co-localizing with 53BP1 and USP28 in ~30% of the cell population ( xref ), suggesting that 53BP1, USP28 and p53 interact with each other after a stressed mitosis, consistent with the known interaction between 53BP1 and p53 or USP28 ( xref ; xref ; xref )."

sparser
"These data show that 53BP1 binds independently to p53 and USP28 via distinct BRCT domain surfaces and pointed toward a potential cooperative role for USP28-53BP1 complexes in p53 regulation."