{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nVAV3 is a multi‐domain guanine nucleotide exchange factor for Rho/Rac family GTPases that plays a pivotal role in immune and hematopoietic cell signaling as well as in platelet function. In lymphocytes, VAV3 facilitates B‐cell receptor–mediated activation by promoting phosphoinositide 3‐kinase activity through Rac1, thereby sustaining phosphatidylinositol‐3,4,5‐trisphosphate production, calcium flux, and c‐Jun N‐terminal kinase activation. In T cells, its recruitment to the immunological synapse via interaction with SLP‑76 is critical for optimal nuclear factor of activated T cells (NFAT) activation, and in platelets VAV3 becomes rapidly tyrosine phosphorylated after immunoreceptor activation—acting redundantly with other VAV proteins to modulate phospholipase Cγ2–dependent responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nVAV3 has emerged as an oncogenic signaling hub and nuclear receptor coactivator in a range of solid tumors. In prostate cancer, for example, its overexpression enhances androgen receptor transcriptional activity—even under conditions of low ligand availability—through cooperation with the PI3K‐Akt cascade and by promoting AR intermolecular (N‑/C‑terminal) interactions. Similarly, in glioblastoma, breast, colorectal, gastric, ovarian, pancreatic, and endometrial cancers VAV3 drives tumor cell proliferation, migration, invasion, and chemoresistance by modulating Rac1‐dependent cytoskeletal dynamics and by regulating downstream signaling pathways (including MAPK/ERK, JNK, and NF‑κB). Moreover, specific isoforms such as the truncated VAV3.1 are associated with cancer stem cell features, metastatic dissemination, and poor clinical outcome, thus identifying VAV3 as a promising candidate for targeted intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe functional versatility of VAV3 is underpinned by its modular structure. Its calponin homology (CH), Dbl homology (DH), pleckstrin homology (PH), and SH2/SH3 domains enable regulated engagement with diverse adaptor proteins. For instance, binding of the adaptor APS to the CH domain alleviates autoinhibition and enhances VAV3 tyrosine phosphorylation, thereby boosting its transforming potential. In addition, VAV3 modulates cytoskeletal organization to influence cell adhesion and migration, as illustrated by its ability to enhance endothelial barrier resistance via Rap1 activation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in immune and oncogenic pathways, VAV3 also participates in metabolic and epithelial processes. In studies of adipose and pancreatic tissues from type 2 diabetes patients, altered VAV3 expression is linked to differential regulation of genes involved in neuronal and metabolic functions. Likewise, in cystic fibrosis, aberrantly elevated apical VAV3 expression in airway epithelia promotes fibronectin deposition and active integrin clustering, thereby facilitating pathogenic bacterial adhesion."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kazunori Inabe, Masamichi Ishiai, Andrew M Scharenberg, et al. 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