{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTYROBP (also known as DAP12) is a transmembrane adaptor protein that couples diverse cell‐surface receptors—including TREM2, TREM1, KIRs and others—to intracellular immunoreceptor tyrosine‐based activation motifs (ITAMs), thereby mediating activating signals in innate immune cells. Its association with receptors on microglia, macrophages, dendritic cells, natural killer cells and osteoclasts orchestrates a range of functions such as phagocytosis, cytokine production, cell proliferation, differentiation and migration. In addition, TYROBP signaling contributes to diverse physiological responses, from modulation of pain‐related microglial gene expression in nerve injury to the regulation of receptor surface expression and intracellular trafficking that fine‐tunes effector cell functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nWithin the central nervous system, TYROBP‐mediated signaling is critical for proper microglial homeostasis. Genetic disruptions or mutations affecting TYROBP alter receptor complex formation—most notably with TREM2—which in turn impairs microglial activation and shifts these cells from a homeostatic to a disease‐associated state. Such alterations are directly implicated in neurodegenerative conditions, including Nasu–Hakola disease and early‐onset Alzheimer’s disease, where reduced or aberrant TYROBP activity leads to dysregulated microglial inflammatory responses and defective repair mechanisms."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOutside the CNS, TYROBP plays a pivotal role in regulating innate immune functions that affect bone remodeling, tumor immunity, and systemic inflammatory disorders. In skeletal tissues, loss‐of‐function mutations in TYROBP contribute to defective osteoclast differentiation and impaired bone resorption—phenomena central to diseases such as Nasu–Hakola disease and postmenopausal osteoporosis. Likewise, aberrant TYROBP expression has been linked to aggressive phenotypes in various cancers (for example, in clear cell renal cell carcinoma, osteosarcoma and low‐grade glioma) by modulating the tumor microenvironment and immune cell recruitment. In inflammatory conditions such as rheumatoid arthritis and inflammatory bowel disease, heightened TYROBP‐dependent signaling exacerbates leukocyte activation and cytokine release, suggesting that targeting its pathway may offer therapeutic benefits."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Juha Paloneva, Tuula Manninen, Grant Christman, et al. 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