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this study shows that 53BP1 is required for three-dimensional organization of the immunoglobulin heavy chain locus and provides a plausible explanation for the link with 53BP1 enforcement of deletional immunoglobulin class switch recombination
Genomic instability can be rescued by the deletion of Trp53bp1, which encodes the DNA damage response factor 53BP1, and mice expressing RING-less BRCA1 (show BRCA1 Proteins) do not show an increased susceptibility to tumors in the absence of 53BP1.
Unlike directly induced DSBs, secondary DSBs were not efficiently repaired, although Rad51 (show RAD51 Proteins) and 53BP1 were recruited to these sites. H2AX (show H2AFX Proteins) was dramatically stabilized in response to DSBs directly caused by gamma-rays, enabling gammaH2AX (show H2AFX Proteins) foci formation and DSB repair, whereas H2AX (show H2AFX Proteins) was barely stabilized in response to secondary DSBs, in which gammaH2AX (show H2AFX Proteins) foci were small and DSBs were not efficiently repaired
Study showed that mammalian cells use microtubules in the cytoplasm to promote the mobility of sites of DNA damage in the nucleus; molecular details of this process remain to be determined, the main players, including the MOB (show SGMS1 Proteins) domain of 53BP1, the linker of the nucleoskeleton, and cytoskeleton complex, kinesins, and microtubules are now known, allowing further study.
These experiments define a novel requirement for 53BP1 in the fusions of DNA-PKcs (show PRKDC Proteins)-deficient telomeres throughout the cell cycle.
Study concludes that only the 53BP1 status in DNA lesions, induced by UVA or gamma-rays, is affected by A-type lamin (show LMNA Proteins) deficiency, which was not observed for heterochromatin-related proteins HP1beta (show CBX1 Proteins) and BMI1 (show BMI1 Proteins).
Binding of 53BP1 to methyl K810 occurs on E2 promoter binding factor (show E2F1 Proteins) target genes and allows pRb (show PGR Proteins) activity to be effectively integrated with the DNA damage response.
study uncovers novel ATM (show ATM Proteins)-independent functions for 53BP1 in the suppression of oncogenic translocations and in radioprotection
Study concludes that 53BP1 promotes productive class switch recombination and suppresses mutagenic DNA repair through distinct phosphodependent interactions with RIF1 and PTIP (show PAXIP1 Proteins).
Thus, RIF1 and 53BP1 cooperate to block DSB resection to promote NHEJ in G1, which is antagonized by BRCA1 in S phase to ensure a switch of DSB repair mode to homologous recombination
BRCA1 promotes PP4C-dependent 53BP1 dephosphorylation and RIF1 release, directing repair toward homologous recombination.
Co-localization of gammaH2AX (show H2AFX Proteins) and 53BP1 indicates promotion of (in)effective nonhomologous end-joining repair mechanisms at sites of DSB. Moreover, gammaH2AX (show H2AFX Proteins)/53BP1 foci distribution presumably reveals a non-random spatial organization of the genome in MDS (show PAFAH1B1 Proteins) and AML (show RUNX1 Proteins).
Results provide evidence that 53BP1 is involved in breast cancer cells resistance for PARP inhibitor; its depletion causes resistance in ATM (show ATM Proteins)-deficient tumor cells.
Ubiquitin ligases RNF168 (show RNF168 Proteins), RNF169 (show RNF169 Proteins), and RAD18 (show RAD18 Proteins) specifically bind histone H2A Lys13/15-ubiquitylated nucleosomes. 53BP1 chromatin recruitment may be activated by RNF168 (show RNF168 Proteins) and blocked by RNF169 (show RNF169 Proteins) and RAD18 (show RAD18 Proteins).
53BP1 embodies two distinct activities: it can act as a DNA repair factor on the chromatin that flanks double-strand DNA repairs, and it promotes optimal p53 (show TP53 Proteins) activity.
Ras-induced senescent cells are hindered in their ability to recruit BRCA1 and 53BP1 to DNA damage sites. Whereas BRCA1 is downregulated at transcripts levels, 53BP1 loss is caused by activation of cathepsin L-mediated degradation of 53BP1 protein. we discovered a marked downregulation of vitamin D receptor (VDR) during OIS, and a role for the vitamin D/VDR axis regulating the levels of these DNA repair
53BP1-USP28 (show USP28 Proteins) cooperation is essential for normal p53 (show TP53 Proteins)-promoter element interactions and gene transactivation-associated events, yet dispensable for 53BP1-dependent DNA double-strand repair regulation.
TIP60 (show KAT5 Proteins) complex regulates bivalent chromatin recognition/modification by 53BP1 through direct H4K20me binding and H2AK15 acetylation.
findings identify TIRR as a new factor that influences double-strand break repair using a unique mechanism of masking the histone methyl-lysine binding function of 53BP1
Deficiency of 53BP1 inhibits the radiosensitivity of colorectal cancer.
May have a role in checkpoint signaling during mitosis. Enhances TP53-mediated transcriptional activation. Binds to sites of DNA damage. Plays a role in the response to DNA damage (By similarity).
tumor protein p53 binding protein 1
, tumor protein p53 binding protein, 1
, tumor suppressor p53-binding protein 1-like
, tumor protein p53 binding protein 1 (predicted), 5 prime
, tumor protein p53 binding protein 1 (predicted), 3 prime
, murine p53-binding protein
, p53-binding protein 1
, transformation related protein 53 binding-protein 1
, tumor suppressor p53-binding protein 1
, tumor protein 53-binding protein, 1
, tumor protein p53-binding protein, 1
, transformation related protein 53 binding protein 1