{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nWDR5 is an evolutionarily conserved WD40‐repeat protein that plays a central role in chromatin regulation. Structural and biochemical studies show that WDR5 directly associates with histone H3 tails—including di‐ and trimethylated lysine 4—and recognizes conserved protein motifs (such as the “Win” motif in MLL/SET1 family members) to promote proper assembly of histone methyltransferase complexes. This scaffolding function is essential for the global deposition of H3K4 trimethylation, activation of critical developmental genes (for example, HOX genes), and normal vertebrate development."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, WDR5 is frequently overexpressed and functions as an oncogenic cofactor by reprogramming gene expression via its role in H3K4 methylation. It is co-opted by long noncoding RNAs (for example, GClnc1, HOXD‐AS1, and GCAWKR) that act as molecular scaffolds to recruit WDR5 along with histone acetyltransferases, thereby directing specific histone modifications and activating target genes involved in cell proliferation, self-renewal, chemoresistance, and metastasis across malignancies such as acute myeloid leukemia, bladder, prostate, gastric, colorectal cancers, and neuroblastoma. WDR5 also partners with transcription factors like MYC to secure chromatin binding and drive oncogenic transcriptional programs, and its inhibition by small-molecule antagonists (e.g., OICR‐9429) disrupts these protein–protein interactions, establishing WDR5 as a promising therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in chromatin modification, WDR5 is also implicated in several non‐transcriptional and structural cellular processes. It contributes to the antiviral response by mediating the assembly of virus‐induced signaling complexes, and it facilitates the nuclear egress of viral capsids in cytomegalovirus infection. WDR5 further influences cell polarity, nuclear deformability, and cytokinesis—localizing to key structures such as the midbody during abscission—and modulates cell migration in three-dimensional environments. In addition, interactions with transcription factors (for instance, SRY), participation in self‐regulatory loops, maintenance of protein structural integrity through specialized hydrogen-bond networks, and the mediation of environmental effects (as seen with bisphenol A exposure in endometriosis) further underscore the multifaceted roles of WDR5 in both physiological and pathological settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "32", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joanna Wysocka, Tomek Swigut, Thomas A Milne, et al. 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