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Data suggest that X-linked inhibitor of apoptosis (XIAP)XIAP acts as a multifunctional pro-metastatic protein in skin melanomas and that XIAP may serve as a therapeutic target for these melanomas.
XIAP is phosphorylated by GSK3 at threonine 180, and that an alanine mutant (XIAP(T180A)) exhibits decreased Wnt3a activity compared to wild-type XIAP in cultured human cells and in Xenopus embryos.
study uncover that the RING domain of XIAP supports c-Myc protein stability, providing insight into the molecular mechanism and role of c-Myc overexpression in cancer progression.
The X-linked inhibitor-of-apoptosis protein (XIAP) was directly targeted and suppressed by miR-122 in HAECs, and more importantly, XIAP knockdown diminished miR-122 effect on apoptosis, thus establishing XIAP as a prominent target that mediates miR-122 regulation of the apoptosis of HAECs.
p53 activation and XIAP suppression were two independent ways that ASPP2 enhance the sensitivity of chemotherapy.
In summary, the authors provide novel lines of evidence suggesting that early-branched eukaryote Entamoeba histolytica may promote apoptosis of human colon cells by modulating, in part, the host microRNome which highlight an unexpected role for miRNA-643/XIAP axis in the host cellular response to parasites infection.
circ_0067997 was identified to be an oncogene in GC by regulating miR-515-5p/XIAP axis
data indicate that active caspase-3 and XIAP could be substantial diagnostic markers for breast cancer patients.
High XIAP expression is associated with proliferation, migration, invasion and epithelial-mesenchymal transition of esophageal cancer.
results revealed that circPAN3 may be a key mediator for chemoresistance of AML cells, which may depend on the circPAN3-miR-153-5p/miR-183-5p-XIAP axis.
The authors defined a critical role of XIAP in transducing MAPK signals to NFkB downstream of MAP kinase interacting serine-threonine kinase, possibly explaining the survival and oncogenic phenotypes associated with MAP kinase interacting serine-threonine kinase signaling.
High XIAP expression is associated with Malignant Grade in Prostate Cancer.
XIAP enhanced cancer cell proliferation, viability, and colony formation in vitro via suppression of p62. In addition, we demonstrated that XIAP-enhanced tumor growth is dependent on depletion of p62 in vivo. Herein, we have therefore delineated a novel mechanism by which XIAP contributes to development and progression of breast and colon carcinoma
WT1 loss positively affected the expression of the X-linked inhibitor of apoptosis protein, XIAP, and genetic or chemical inhibition with embelin (a XIAP inhibitor) significantly restored sensitivity to gamma-radiation in both T-cell acute lymphoblastic leukemia cell lines and patient-derived xenografts.
high expression of XIAP was correlated with ovarian cancer paclitaxel resistance
Multiple Hsp70-binding sites were mapped XIAP, suggesting that it is a direct, physical Hsp70 client.
Overexpression of survivin in gallbladder cancer suggests its possible role and association with poor prognosis. But XIAP has not been found to be associated with gallbladder carcinogenesis.
XIAP limits autophagic degradation of Sox2 and is a therapeutic target in nasopharyngeal carcinoma stem cells.
Upregulation of XIAP in Colorectal Cancer Cells (CRC) is responsible for the acquired resistance to oxaliplatin. Furthermore, miR-122 reversed oxaliplatin resistance in CRC by targeting XIAP.
Results demonstrate that XIAP-regulated Erks/nucleolin/RhoGDIbeta axis promoted BC invasion and lung metastasis.
IAP inhibition or loss of both cIAP2 and XIAP resulted in a strong blockage in autophagic flux and mitophagy, suggesting that XIAP deficiency may also drive Crohn's Disease due to defects in autophagy.
It was demonstrated that cryopreservation reduces the expression of XIAP and decreases the survival rate of blastocysts.
Differentiation of macrophages increased the expression of pro-inflammatory cytokines but reduced RipK1-dependent cell death and the RipK3-caspase-8 interaction. The expression of the anti-apoptotic mediators, X-linked inhibitor of apoptosis protein (XIAP) and caspase-like apoptosis regulatory protein (cFLIPL), also increased in differentiated macrophages, which inhibited caspase activation.
mRNA and protein expressions of XIAP were decreased via siRNA targetting, which leads to increases in cell apoptosis and caspase-3 and caspase-9 activity. It also contributed to the reduced tumor size and tumor weight in a nude mice model of esophageal cancer.
The neuron-specific form of FAIM protein (FAIM-L) is a death receptor antagonist that stabilizes XIAP protein levels, thus preventing death receptor-induced neuronal apoptosis. Here we show that FAIM-L modulates synaptic transmission, prevents chemical-LTD induction in hippocampal neurons, and thwarts axon degeneration after nerve growth factor (NGF) withdrawal.
These data reveal how, upon XIAP deficiency, a TLR-TNF-TNFR2 axis drives cIAP1-TRAF2 degradation to allow TLR or TNFR1 activation of RIPK3-caspase-8 and IL-1beta. This mechanism may explain why XIAP-deficient patients can exhibit symptoms reminiscent of patients with activating inflammasome mutations.
There was a significantly decreased percentage of IL-17A-producing CD4 T cells in mice receiving Tregs from xIAP mice. xIAP appears dispensable for the generation of induced Treg cells as well as function of natural Treg cells. There appeared to be a role of xIAP in generation of IL-17-producing cells from either naive CD4 T cells or Treg cells.
Drugs targeting XIAP and cIAP1/2 may be effective for osteosarcoma patients whose tumors express abundant RIPK1 and contain high levels of TNFalpha.
Deletion of XIAP switches cell death away from necrosis to apoptosis.
These results indicate that XIAP plays an important physiologic role in regulating sublethal CASP-3 activity within central neurons and thereby facilitates synaptic plasticity and memory acquisition.
XIAP antagonizes the switch from TNFalpha-induced apoptosis to necroptosis in mouse neutrophils.
Results show that XIAP binds to the C terminus of Ptch1 and mediates the death-dependent function of Ptch1.
XIAP modulates ubiquitylation of RIP1 and suppresses RIP3-dependent cell death and inflammasome activation in response to TNF-signaling in innate immune cells.
XIAP deficiency selectively impaired B-cell chronic lymphocytic leukemia/lymphoma 10 (BCL10)-mediated innate responses to dectin-1 ligands but did not affect responses to various Toll-like receptor agonists.
XIAP mRNA level was also reduced in the BRE-depleted cells, but the level of reduction was less profound than that of the protein level. However, BRE could not delay protein turnover of XIAP.
Identify xIAP and cIAP1 as molecular targets of ceramide and show ceramide analog LCL85 is an effective sensitizer in overcoming resistance of metastatic colon and breast cancers to apoptosis induction to suppress metastasis in vivo.
XIAP-/- DRG sensory neurons degenerate more rapidly and contain more active caspase-3.
XIAP ubiquitylates RIPK2 and recruits the linear ubiquitin chain assembly complex to NOD2
This gene encodes a protein that belongs to a family of apoptotic suppressor proteins. Members of this family share a conserved motif termed, baculovirus IAP repeat, which is necessary for their anti-apoptotic function. This protein functions through binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2 and inhibits apoptosis induced by menadione, a potent inducer of free radicals, and interleukin 1-beta converting enzyme. This protein also inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. Mutations in this gene are the cause of X-linked lymphoproliferative syndrome. Alternate splicing results in multiple transcript variants. Pseudogenes of this gene are found on chromosomes 2 and 11.
E3 ubiquitin-protein ligase XIAP
, IAP-like protein
, X-linked IAP
, baculoviral IAP repeat-containing protein 4
, inhibitor of apoptosis protein 3
, Baculoviral IAP repeat-containing protein 4
, X-linked inhibitor of apoptosis protein
, baculoviral IAP repeat-containing 4
, baculoviral IAP-repeat containing protein 4
, IAP homolog A
, apoptosis inhibitor 3
, apoptosis inhibitor protein 3
, baculoviral IAP repeat containing 8