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NPM1 (show GJA1 Proteins)-dependent nucleolar PIDDosome is a key initiator of the caspase-2 (show CASP2 Proteins) activation cascade.
PIDD acts as a critical switcher between the NF-kappabeta (show NFKB1 Proteins) transcription pathway and radiation-induced apoptosis
The tumor-modulatory effects of Caspase-2 (show CASP2 Proteins) and Pidd1 do not require the scaffold protein (show HOMER1 Proteins) Raidd (show CRADD Proteins)
Loss of PIDD leads to an impaired inflammatory response after DNA damage.
Caspase 2 (show CASP2 Proteins) activity can be induced in neurons from PIDD-null mice, and NGF (show NGFB Proteins) deprivation or Abeta (show APP Proteins) use caspase 2 (show CASP2 Proteins) and RAIDD (show CRADD Proteins) to execute death of these neurons.
P450 (show POR Proteins) levels were higher in female DES (show DES Proteins)-treated p53 (show TP53 Proteins)+/- mice compared to treated wild type mice.
Results suggest that at least one alternative PIDDosome-independent mechanism of caspase-2 (show CASP2 Proteins) activation exists in mammals in response to DNA damage.
PIDD does not play an essential role for all p53 (show TP53 Proteins)-mediated or p53 (show TP53 Proteins)-independent apoptotic pathways.
Whole exome sequencing (WES) of an affected fetus, and subsequent Sanger sequencing of the second fetus, revealed a homozygous frameshift variant in CRADD (show CRADD Proteins), which encodes an adaptor protein that interacts with PIDD and caspase-2 (show CASP2 Proteins) to initiate apoptosis
NPM1 (show NPM1 Proteins)-dependent nucleolar PIDDosome is a key initiator of the caspase-2 (show CASP2 Proteins) activation cascade.
PIDD expression was lower in HCC (show FAM126A Proteins) tissues and HCC (show FAM126A Proteins) cell lines, compared with the adjacent non-tumorous tissues and LO2 normal hepatocytes. PIDD could serve as an independent prognostic factor to predict the survival of HCC (show FAM126A Proteins) patients. PIDD facilitated cell cycle progression and accelerated cell proliferation in HepG2 cells, while overexpression of PIDD resulted in cell cycle arrest at G1 phase in Hep3B cells.
By sequestering PIDD at the kinetochore, BubR1 (show BUB1B Proteins) acts to delay PIDDosome formation until the next cycle, defining a new mechanism by which cells evade apoptosis during mitosis.
The ATM (show ATM Proteins) phosphorylation of the PIDD DD enables a binary switch through which cells elect to survive or die upon DNA injury.
PIDD performs key functions upon UV irradiation, including TLS (show FUS Proteins), NHEJ, NF-kappaB (show NFKB1 Proteins) activation and cell death.
Hsp90 (show HSP90 Proteins) has a major role in controlling PIDD functional activity.
a new splicing variant of PIDD named PIDD4 is reported.
point mutations on RAIDD (show CRADD Proteins) (R147E) and on PIDD (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed
Total caspase-2 (show CASP2 Proteins) is upregulated during tumour progression in renal cell carcinomas.
The protein encoded by this gene contains a leucine-rich repeat and a death domain. This protein has been shown to interact with other death domain proteins, such as Fas (TNFRSF6)-associated via death domain (FADD) and MAP-kinase activating death domain-containing protein (MADD), and thus may function as an adaptor protein in cell death-related signaling processes. The expression of the mouse counterpart of this gene has been found to be positively regulated by the tumor suppressor p53 and to induce cell apoptosis in response to DNA damage, which suggests a role for this gene as an effector of p53-dependent apoptosis. Alternative splicing results in multiple transcript variants.
leucine-rich repeat and death domain-containing protein
, p53 protein induced, with death domain
, p53-induced protein with a death domain
, leucine-rich repeats and death domain containing