
NCBI . NLM . NIH . GOV {
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Title[redir]:
An Inhibitor of PIDDosome Formation - PMC
Description:
The PIDDosome—PIDD-RAIDD-caspase-2 complex—is a proapoptotic caspase-activation platform of elusive significance. DNA damage can initiate complex assembly via ATM phosphorylation of the PIDD death domain (DD), which enables RAIDD recruitment to ...
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Keywords {🔍}
bubr, pidd, doi, piddosome, figure, cells, caspase, pubmed, google, scholar, cell, dna, raidd, mitotic, pmc, treated, analyzed, article, damage, interaction, hela, free, kts, harvested, western, blot, post, checkpoint, bub, apoptosis, response, chk, death, recruitment, transfected, inhibition, formation, assembly, shown, aurora, mitosis, protein, control, data, complex, domain, required, cleavage, mefs, figures,
Topics {✒️}
pro-survival nf-kappab pathway c-terminal pidd-cc fragment p53m214k/m214k zebrafish embryos bubr1-pidd dimers/complexes assembled ice/ced-3-related gene pmc beta search supplemental experimental procedures mad2-bubr1-bub3-cdc20 tetramer hpv-harboring hela cells ruth rodriguez-barrueco fas-fadd-caspase-8 sequentially integrates dna-damage pidd-bubr1 dimers/complexes supplementary materials included ich-1/ced homologous protein dna damage-dependent events kt-deficient bubr1e413k mutant maintain bubr1-mediated inhibition negates piddosome-mediated apoptosis anaphase-promoting complex/cyclosome mol cell summary p53-defective cells triggered references allan la aberrant microtubule-kt attachments cooperative/synergistic interactions observed bubr1-mediated mitotic arrest piddosome—pidd-raidd-caspase-2 complex mad2-induced functional switch ir shifted pidd-cc suppress piddosome-mediated apoptosis restored phospho-pidd recruitment stable kinetochore-microtubule attachments piddosome-independent tumor suppression atm/atr-dependent manner transiently transfected gfp-bubr1 proapoptotic caspase-activation platform bubr1-bound pidd dd dna damage-induced phosphorylation dna-damage-induced apoptosis ir-induced dna damage piddosome-dependent apoptotic response caspase-3-dependent apoptotic response bubr1-mediated piddosome control p53-inducible protein 24 hr post-dox tp53−/− hct116 cells pidd death-domain phosphorylation atm-phosphorylated pidd relocates nih grants 5r01ca178162 strong ir-induced interaction
Questions {❓}
- Caspase 2 in apoptosis, the DNA damage response and tumour suppression: enigma no more?
- How does the DDR engage BubR1 and mobilize it to PIDD?
- If not at the KT, where might BubR1 and PIDD initially interact?
- P53-induced protein with a death domain (PIDD): master of puppets?
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