{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUNC93B1 is an evolutionarily conserved, multi–transmembrane domain protein that functions as an essential chaperone in the endoplasmic reticulum, orchestrating the intracellular trafficking and maturation of nucleic acid–sensing Toll‐like receptors (TLRs) such as TLR3, TLR7, TLR8, TLR9, and TLR13. By facilitating the exit of these receptors from the ER and ensuring their proper delivery to endolysosomes – where they often undergo critical proteolytic cleavage to generate active signaling fragments – UNC93B1 ensures robust antiviral and innate immune responses. In human antigen‐presenting cells, even modest alterations in UNC93B1 expression can affect TLR responsiveness, underscoring its central role in innate immune surveillance and interferon regulation."}, {"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": "\nMoreover, UNC93B1 is a key regulator that modulates TLR signaling thresholds to maintain self‐tolerance. Disruption or mutation of UNC93B1 can lead to either impaired interferon responses and susceptibility to viral encephalitis or, conversely, to hyperactivity of TLR7/8 signaling pathways that predispose to autoimmunity, as observed in various lupus phenotypes. These mutations exert receptor‐specific effects, emphasizing that finely tuned UNC93B1 interactions are critical to prevent aberrant cytokine production and autoimmune disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role in TLR trafficking, UNC93B1 also participates in the regulation of other critical innate immune processes. It interacts with key signaling molecules such as STIM1 and STING to control calcium flux and antigen cross‐presentation in dendritic cells, and to temper cytosolic DNA–induced responses by targeting STING for autophagy‐lysosome degradation. These interactions serve as pivotal checkpoints that prevent excessive immune activation during viral infections."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition, UNC93B1 influences the development and maintenance of specific immune cell subsets. Its regulation of intracellular TLR localization affects the balance of B‐cell tolerance checkpoints, while its role in sorting and trafficking impacts other cell types critical to immune homeostasis. For instance, in the context of hematopoietic stem cell transplantation, genetic variation in UNC93B1 has been associated with improved outcomes, reflecting its broader immunomodulatory functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies further reveal that UNC93B1 may have roles beyond innate immunity. Elevated expression of UNC93B1 has been observed in oral squamous cell carcinoma, where it appears to promote tumoral growth through modulation of cytokine secretion, suggesting potential oncogenic functions. In addition, its high expression in the heart and association with clinical outcomes highlight emerging roles in non‐immune tissues as well as in post–transplant settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Armanda Casrouge, Shen-Ying Zhang, Céline Eidenschenk, et al. 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