ArticleCommunications biology2021
Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- LIN28A-Dependent Kinome and Phosphoproteome Reprogramming Promotes Imatinib Resistance.Molecular & cellular proteomics : MCP · 2026Article
- Targeting RNA binding proteins with small-molecule inhibitors: Advances, challenges, and therapeutic opportunities.Acta pharmaceutica Sinica. B · 2026Review
- Article
- mRNA recruitment by G3BP1 condensates is regulated by Caprin1 but requires G3BP1 binding to mRNA.Scientific reports · 2025Article
- Developing novel Lin28 inhibitors by computer aided drug design.Cell death discovery · 2025Article
- Exosome miRNA sorting controlled by RNA-binding protein-motif interactions.Extracellular vesicles and circulating nucleic acids · 2025Review
- YBX1: A Multifunctional Protein in Senescence and Immune Regulation.Current issues in molecular biology · 2024Review
- Lin28a forms an RNA-binding complex with Igf2bp3 to regulate mCell proliferation · 2024Article
- Liver cancer initiation requires translational activation by an oncofetal regulon involving LIN28 proteins.The Journal of clinical investigation · 2024Article
- The LIN28B-let-7-PBK pathway is essential for group 3 medulloblastoma tumor growth and survival.Molecular oncology · 2023Article
- PEPseq quantifies transcriptome-wide changes in protein occupancy and reveals selective translational repression after translational stress.Nucleic acids research · 2023Article
- Non-Coding RNAs Are Implicit in Chronic Myeloid Leukemia Therapy Resistance.International journal of molecular sciences · 2022Review
- RNANetMotif: Identifying sequence-structure RNA network motifs in RNA-protein binding sites.PLoS computational biology · 2022Article
- YB-1 unwinds mRNA secondary structures in vitro and negatively regulates stress granule assembly in HeLa cells.Nucleic acids research · 2021Article
- Lin28A/CENPE Promoting the Proliferation and Chemoresistance of Acute Myeloid Leukemia.Frontiers in oncology · 2021Article
Corrections and comments
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Authors and funding
17 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA-binding protein Lin28 (Lin28a) is an important pluripotency factor that reprograms translation and promotes cancer progression. Although Lin28 blocks let-7 microRNA maturation, Lin28 also binds to a large set of cytoplasmic mRNAs directly. However, how Lin28 regulates the processing of many mRNAs to reprogram global translation remains unknown. We show here, using a structural and cellular approach, a mixing of Lin28 with YB-1 (YBX1) in the presence of mRNA owing to their cold-shock domain, a conserved β-barrel structure that binds to ssRNA cooperatively. In contrast, the other RNA binding-proteins without cold-shock domains tested, HuR, G3BP-1, FUS and LARP-6, did not mix with YB-1. Given that YB-1 is the core component of dormant mRNPs, a model in which Lin28 gains access to mRNPs through its co-association with YB-1 to mRNA may provide a means for Lin28 to reprogram translation. We anticipate that the translational plasticity provided by mRNPs may contribute to Lin28 functions in development and adaptation of cancer cells to an adverse environment.
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