{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRBCK1 (also known as HOIL‐1) functions as a critical E3 ubiquitin ligase and is an essential component of the linear ubiquitin chain assembly complex (LUBAC) that modulates inflammatory and innate immune signaling. It plays a dual role in fine‐tuning nuclear factor‐κB (NF‐κB) activation by facilitating cell type–specific cytokine responses – for example, its deficiency leads to impaired LUBAC stability and abnormal IL‐1β responses underlying autoinflammatory disorders, while in mononuclear cells its loss results in hyperresponsiveness. RBCK1 also catalyzes the polyubiquitination and proteasomal degradation of key immune regulators such as interferon regulatory factor 3 (IRF3), thereby acting as a negative feedback mechanism during viral infection. Moreover, regulated cleavage of RBCK1 by MALT1 further dampens NF‐κB activation, and pharmacological targeting of LUBAC is being explored based on these mechanistic insights."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the muscle and heart, mutations or deficiencies in RBCK1 have been linked to polyglucosan body myopathy and cardiomyopathy. Loss‐of‐function mutations in RBCK1 disrupt its ubiquitin ligase activity needed for proper post‐translational modifications of glycogen and related substrates, leading to toxic polyglucosan deposits, progressive myopathy, and cardiac dysfunction. Clinical reports in patients with RBCK1 mutations further reveal that these disruptions can also be associated with autoinflammation and combined immunodeficiency."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer, RBCK1 exerts multifaceted roles that vary with the tumor context. In estrogen receptor–positive breast cancer, RBCK1 supports cell cycle progression by facilitating transcription of ERα and cyclin B1, while its interaction with HOXA1 and regulators such as FKBPL modulates NF‐κB activity and endocrine responsiveness. In renal cell carcinoma, RBCK1 promotes p53 polyubiquitination and degradation, thereby favoring proliferation, and in colorectal cancer its up‐regulation contributes to chemoresistance and maintenance of stemness features. Additionally, emerging data suggest that RBCK1 may influence hypoxia‐induced signaling and aggressive phenotypes in triple‐negative breast cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical roles in immunity and cancer, RBCK1 also participates in the regulation of transcription and cellular homeostasis through interactions with diverse partners. It binds to transcription factors such as Eya1 to modulate developmental programs and has its activity finely regulated by a naturally occurring splice variant, RBCK2, which sequesters RBCK1 and alters its subcellular localization and ubiquitin ligase activity. In addition, RBCK1 targets other nuclear receptors like the pregnane X receptor for degradation, and recent studies indicate it may also modulate allergic responses in nasal epithelium and govern ferroptosis sensitivity in pancreatic cancer via the degradation of mitochondrial regulators such as mitofusin 2. Furthermore, RBCK1 dimerization (together with related proteins like SHARPIN) adds an additional layer to its regulatory repertoire."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yang Tian, Yan Zhang, Bo Zhong, et al. 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