{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nY‐box binding protein‑1 (YBX1) is an evolutionarily conserved nucleic acid–binding protein characterized by its cold shock domain that enables interactions with DNA and RNA. It functions as a multifunctional regulator of gene expression by modulating transcription, translation, mRNA splicing, and even participating in DNA repair and viral replication. In fact, early studies demonstrated that YBX1 forms oligomers and associates with key repair factors—such as stimulating base excision repair through its interaction with NEIL2—thereby safeguarding genome integrity while also being co‐opted by viruses to support their replication cycles."}, {"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": "\nYBX1 exerts profound effects on cell proliferation and oncogenic signaling. Its regulated phosphorylation (for example, by Akt at Ser102) promotes nuclear translocation where it transcriptionally activates key cell cycle regulators—including cyclins and EMT‐inducing factors such as Snail1 and MET—to drive tumor growth and metastasis. These studies also link YBX1 with enhanced cap‑independent translation and suggest that its upregulation, via factors like Twist, underpins drug resistance and cancer stem cell maintenance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in classical gene regulation, YBX1 is instrumental in coordinating the cellular stress response and RNA homeostasis. Under stress conditions, YBX1 promotes the assembly of stress granules by directly binding to the 5′ untranslated region of mRNAs encoding stress‐granule nucleators such as G3BP1. In addition, by undergoing liquid–liquid phase separation, YBX1 selectively recruits small noncoding RNAs—including tRNA‐derived fragments and microRNAs—into extracellular vesicles, thereby influencing intercellular communication and the purging of excess RNAs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA complex network of noncoding RNAs further fine‑tunes YBX1 function. Specific tRNA‑derived fragments can displace oncogenic mRNA transcripts from YBX1, contributing to tumor‐suppressive effects. Moreover, several long noncoding RNAs—including GAS5, HULC, MIR22HG, LNCAROD, TP53TG1—and circular RNAs such as circFAT1(e2) interact with YBX1 to regulate its turnover, post‑translational modification, subcellular localization, and transcriptional activity. These RNA–protein interactions modulate processes including cell cycle progression, epithelial–mesenchymal transition (EMT), and chemoresistance in multiple cancer types."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nYBX1 additionally contributes to oncogenesis and therapeutic resistance across a variety of malignancies. By transcriptionally upregulating genes that promote cell survival, stemness, and multidrug resistance (including MDR1, MET, CD44, and BCL2), YBX1 integrates into key oncogenic signaling pathways such as ERK and PI3K/AKT. Its upregulation by oncogenic factors like Twist, c‑Myc, and p73—as well as its stable incorporation into transcriptional complexes with coactivators like APE1 and chromatin regulators—further consolidates its role in tumor progression, metastasis (for example, through EMT in prostate cancer and osteosarcoma), and the maintenance of leukemic cell survival."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "31", "end_ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Per S Holm, Stephan Bergmann, Karsten Jurchott, et al. 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