{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMYD88 is a central adaptor protein that mediates intracellular signaling from Toll‐like and interleukin‐1 receptors. Upon receptor engagement, MYD88 recruits interleukin‐1 receptor–associated kinases to nucleate supramolecular “myddosome” complexes that activate downstream effectors such as nuclear factor–κB, mitogen‐activated protein kinases, and interferon regulatory factors. Structural studies have revealed that MYD88’s Toll/IL‐1 receptor (TIR) domain forms atypical left‐handed helical oligomers with IRAK4 and IRAK2, and that alternative splicing and regulated proteasomal degradation of MYD88 further modulate its signal‐transducing capacity."}, {"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 addition to its canonical role, MYD88 is pivotal in orchestrating host immune responses and maintaining inflammatory homeostasis. By bridging pattern‐recognition receptors with downstream signaling cascades, it directs the production of type I interferons, proinflammatory cytokines and chemokines in response to bacterial, viral, and endogenous stimuli. Loss‐of‐function studies and observations in MYD88‐deficient patients underscore its necessity for defense against pyogenic bacteria and for the regulation of innate inflammatory responses. Moreover, MYD88 functions in nontraditional contexts—including endothelial cell activation and immunoglobulin class switching via receptors such as TACI—further attesting to its versatility in both health and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulated MYD88 signaling—most notably through recurrent gain‐of‐function mutations such as L265P—is a hallmark of several B‐cell malignancies and related lymphoproliferative disorders. In diseases including activated B‐cell–like diffuse large B‐cell lymphoma, Waldenström macroglobulinemia, vitreoretinal lymphoma, marginal zone lymphoma, and other central nervous system and ocular lymphomas, mutant MYD88 drives constitutive NF–κB activation and supports prosurvival and anti‐apoptotic programs. These oncogenic activities have spurred the development of targeted inhibitors aimed at disrupting MYD88 dimerization or its downstream interactions, offering promising personalized therapeutic strategies against tumors driven by aberrant MYD88 signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joo Y Lee, Jianping Ye, Zhanguo Gao, et al. 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