ArticleNucleic acids research2020
Structural basis of DNA binding to human YB-1 cold shock domain regulated by phosphorylation.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 47 citations in OpenAlex.
- Loss of Erbin in tubular epithelial cells sensitizes mice to acute kidney injury and aggravates renal fibrosis.The EMBO journal · 2026Article
- Prioritizing Candidate YB‑1 Cold Shock Domain Ligands via 5D-ElectroShape and Boltz Generative Cofolding.ACS omega · 2026Article
- The Role of Cold Shock Protein (CSP) Gene Family in Yak (Bos grunniens) for High-Altitude Adaptation: Genome-Wide Identification and Analysis.Animal genetics · 2026Article
- Phosphorylation of YBX1 in the Kidneys is Altered in Legumain Knockout-Mice.Journal of proteome research · 2026Article
- Y-box binding protein-1 at the crossroads of DNA damage response and tumor immune evasion.JNCI cancer spectrum · 2026Review
- YB-1 AP-CSD Forms Cross-β Amyloid Fibrils Without Secondary-Structure Conversion In Vitro.International journal of molecular sciences · 2026Article
- Discovery of a Novel Small-Molecule Modulator for Full-length YB-1 Protein via Integrated Computational and in vitro Biophysical Approaches.Applied biochemistry and biotechnology · 2026Article
- Hypoxic mesenchymal stem cell-Derived Exosomal circPTP4A2 improves granulosa cell mitochondrial function via YBX1.Cellular and molecular life sciences : CMLS · 2026Article
- Marginal Stability of the YB1 Cold-Shock Domain in Cells Enables Binding of Multiple Nucleic Acids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- YBX1 as an adaptive RNA hub in cancer: linking state-dependent RNA regulation to tumor immunity, metabolic reprogramming, and therapy resistance.Frontiers in immunology · 2026Review
- Multifaceted functions of Y‑box binding protein 1 in RNA methylated modifications (Review).Molecular medicine reports · 2025Review
- YBX1 regulation of alveolar type II epithelial cells in idiopathic pulmonary fibrosis: mechanistic insights and small-molecule drug screening.Journal of translational medicine · 2025Article
- Integrative Investigation of Flavonoids Targeting YBX1 Protein-Protein Interaction Network in Breast Cancer: From Computational Analysis to Experimental Validation.Molecular biotechnology · 2025Article
- KAT7-acetylated YBX1 promotes hepatocellular carcinoma proliferation by reprogramming nucleotide metabolism.BMC cancer · 2025Article
- PGC7 regulates maternal mRNA translation via AKT1-YBX1 interactions in mouse oocytes.Cell communication and signaling : CCS · 2024Article
- Role of Csdc2 in Regulating Secondary Hair Follicle Growth in Cashmere Goats.International journal of molecular sciences · 2024Article
- FAK-LINC01089 negative regulatory loop controls chemoresistance and progression of small cell lung cancer.Oncogene · 2024Article
- Comprehensive pan-cancer analysis of YBX family reveals YBX2 as a potential biomarker in liver cancer.Frontiers in immunology · 2024Article
- YB-1 activating cascades as potential targets in KRAS-mutated tumors.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023Review
- TOPK promotes the growth of esophageal cancer in vitro and in vivo by enhancing YB1/eEF1A1 signal pathway.Cell death & disease · 2023Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human Y-box binding protein 1 (YB-1) is a multifunctional protein and overexpressed in many types of cancer. It specifically recognizes DNA/RNA through a cold shock domain (CSD) and regulates nucleic acid metabolism. The C-terminal extension of CSD and the phosphorylation of S102 are indispensable for YB-1 function. Until now, the roles of the C-terminal extension and phosphorylation in gene transcription and translation are still largely unknown. Here, we solved the structure of human YB-1 CSD with a C-terminal extension sequence (CSDex). The structure reveals that the extension interacts with several residues in the conventional CSD and adopts a rigid structure instead of being disordered. Either deletion of this extension or phosphorylation of S102 destabilizes the protein and results in partial unfolding. Structural characterization of CSDex in complex with a ssDNA heptamer shows that all the seven nucleotides are involved in DNA-protein interactions and the C-terminal extension provides a unique DNA binding site. Our DNA-binding study indicates that CSDex can recognize more DNA sequences than previously thought and the phosphorylation reduces its binding to ssDNA dramatically. Our results suggest that gene transcription and translation can be regulated by changing the affinity of CSDex binding to DNA and RNA through phosphorylation, respectively.
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