{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPlatelet‐derived growth factor receptor‐beta (PDGFRB) has emerged as a pivotal regulator of normal tissue development and regenerative homeostasis. PDGFRB‐positive stromal cells in the human endometrium display mesenchymal stem cell properties that likely underlie the organ’s impressive monthly regenerative capacity, while in renal cells PDGFRB and its ligands coordinate mesangial proliferation, extracellular matrix accumulation, and fibrotic responses. Moreover, recent work has highlighted roles for PDGFRB and its PDGF ligands in human neocortical development—modulating radial glia proliferation and migration—and in mesenchymal stem cell fate decisions via PI3K/Akt and ERK pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAberrant PDGFRB signaling is implicated in a broad array of pathological conditions ranging from oncogenesis and fibrotic disorders to neurovascular abnormalities. In several cancers—including pancreatic, renal, and hematologic malignancies—mutant p53 or gene‐fusions drive PDGFRB expression that promotes metastasis, angiogenesis, cell migration, and survival. Multi‐targeted tyrosine kinase inhibitors that suppress PDGFRB activity (for example, anlotinib) demonstrate potent anti-angiogenic effects, while autoantibodies that activate PDGFRB have been associated with fibrotic phenotypes in chronic graft‐versus‐host disease. Furthermore, PDGFRB crosstalk with integrins directs mesenchymal cell migration, and its mutations underlie conditions such as idiopathic basal ganglia calcification, infantile myofibromatosis, and distinct leukemias defined by fusion events. In cancer-associated stroma, PDGFRB expression in subsets of fibroblasts correlates with enhanced invasion, and receptor shedding from brain pericytes has emerged as a biomarker of blood-brain barrier dysfunction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, PDGFRB orchestrates complex signaling networks by integrating extracellular cues with diverse intracellular effectors. Transcriptional regulators such as JUN and JUNB modulate PDGFRB expression—impacting, for instance, lymphoma progression—while in systemic sclerosis, PDGFRB together with Abl mediates fibrotic cascades that respond to imatinib therapy. Its activation in multiple myeloma, prostate, and gastric cancers influences angiogenesis and tumor microenvironment remodeling via downstream pathways (ERK, AKT, and JNK), and proteolytic processing of its ligands further refines its signaling output. Additionally, genetic alterations in PDGFRB contribute to imatinib resistance in chronic myelogenous leukemia and define novel overgrowth syndromes, while structural analyses have elucidated predominantly hydrophobic ligand-binding interfaces and endocytic interactions with partners such as LRP. 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