{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nXIAP is widely recognized as the most potent and bona fide inhibitor of caspases within the inhibitor of apoptosis (IAP) family. Structural and biochemical studies have revealed that XIAP directly binds to and inhibits caspases through its baculoviral IAP repeat (BIR) domains, with both the BIR2 and BIR3 regions playing indispensable roles in restraining caspase‐3, ‐7, and ‐9 activities. In addition, XIAP’s E3 ubiquitin ligase function allows it to target pro‐apoptotic proteins—for example, Smac/DIABLO—for rapid proteasomal degradation, thereby reinforcing a robust antiapoptotic barrier and modulating the all‐or‐none activation of effector caspases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its cell‐intrinsic function as a caspase inhibitor, XIAP is essential for maintaining immune homeostasis. Studies in patients with X‐linked lymphoproliferative syndrome type 2 have shown that mutations in the XIAP gene lead to defective lymphocyte survival and differentiation—with notable reductions in natural killer T‐cell numbers—and a clinical spectrum that includes hemophagocytic lymphohistiocytosis and Crohn‐like inflammatory bowel disease. These findings underscore the critical role of XIAP in orchestrating immune responses and preventing aberrant lymphoproliferation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "11"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond direct caspase inhibition, XIAP plays a central role in innate immune signaling and the modulation of survival pathways. XIAP physically interacts with key adaptor proteins such as RIP2 to facilitate NOD1/2‐dependent activation of NF‑κB, while also controlling the stability and subcellular localization of critical regulators like PTEN—thereby promoting Akt phosphorylation and cell survival. Moreover, XIAP translation is regulated at the level of its internal ribosome entry site (IRES) by RNA‐binding proteins, highlighting an additional layer of control during cellular stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "15"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant XIAP expression has been implicated in the resistance of diverse human cancers to apoptosis. Overexpression of XIAP—often driven by upstream oncogenic pathways or transcriptional regulators such as FOXM1 and modulated by noncoding RNA networks like circPAN3—correlates with reduced tumor cell susceptibility to chemotherapeutic agents in non–small cell lung, breast, pancreatic, and hepatocellular carcinomas, among others. Therapeutic strategies that target XIAP using antisense oligonucleotides, small‐molecule SMAC mimetics, or by interfering with its upstream regulators have been shown to sensitize tumor cells to diverse anticancer treatments."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "25"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nXIAP function is finely tuned by multiple regulatory mechanisms that govern its protein levels and activity in response to intracellular stress signals. Pro‐apoptotic proteins such as ARTS directly bind to and antagonize XIAP, while mitochondrial proteases like Omi/HtrA2 promote its degradation. Furthermore, posttranslational modifications—including S‑nitrosylation—and interactions with metal ions such as copper can destabilize XIAP, thereby lowering the apoptotic threshold in stress‐sensitive cells such as cardiomyocytes and neurons. In addition, endoplasmic reticulum stress triggers signaling cascades that down‐regulate XIAP synthesis while enhancing its proteasomal degradation, highlighting its dynamic regulation in both protective and pathological settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "33"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Marion MacFarlane, Wendy Merrison, Shawn B Bratton, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M207578200"}], "href": "https://doi.org/10.1074/jbc.M207578200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12218061"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12218061"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Yihua Huang, Rebecca L Rich, David G Myszka, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "cIAP1, cIAP2, and XIAP act cooperatively via nonredundant pathways to regulate genotoxic stress-induced nuclear factor-kappaB activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-08-2256"}], "href": "https://doi.org/10.1158/0008-5472.CAN-08-2256"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19223549"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19223549"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Céline Van Themsche, Valérie Leblanc, Sophie Parent, et al. 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