ArticleNucleic acids research2023
Identification of G-quadruplex structures in MALAT1 lncRNA that interact with nucleolin and nucleophosmin.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- AND-Logic-Gated Aptamer Switch for Precise Targeting and Regulation of RNA G-Quadruplexes.Angewandte Chemie (International ed. in English) · 2026Article
- Review
- Article
- G-quadruplex stabilization via small molecules as a potential anti-cancer strategy.Cellular & molecular biology letters · 2026Review
- Multisite phosphorylation of the AML-linked C-terminal of nucleophosmin (NPM1) orchestrates protein stability, DNA binding and charge block-driven phase separation.Nucleic acids research · 2026Article
- Dual-responsive zwitterionic hydrogel microneedle patch for the on-site detection of two alzheimer's disease - related miRNAs.Journal of nanobiotechnology · 2026Article
- FBXO11 suppression rewires an NPM1-centered interactome influencing the progression of myelodysplastic syndrome.The Journal of clinical investigation · 2026Article
- Revealing G4 Structures as Drug Targets: Exploring the Potential of Novel Therapeutic Agents.Research (Washington, D.C.) · 2026Review
- Targeting G-Rich lncRNA and Its Structural Polymorphism With Selective G-Quadruplex Ligands: An NMR Study.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Quadrupia provides a comprehensive catalog of G-quadruplexes across genomes from the tree of life.Genome research · 2025Article
- LncRNA EP300-AS1 interacts with PTBP1 to destabilize PRMT5 mRNA and suppresses NSCLC growth and metastasis.Cell death & disease · 2025Article
- The mechanism by which MALAT1/CREG1 regulates premature rupture of fetal membrane through autophagy mediated differentiation of amniotic fibroblasts.Non-coding RNA research · 2025Article
- RNA G-quadruplex structure targeting and imaging: recent advances and future directions.RNA (New York, N.Y.) · 2025Review
- Regulation of the lncRNANAR molecular medicine · 2025Article
- Landscape and mutational dynamics of G-quadruplexes in the complete human genome and in haplotypes of diverse ancestry.bioRxiv : the preprint server for biology · 2025Article
- Putative G‑Quadruplex Structures in Dysregulated Long Non-coding RNA of Ovarian Cancer and Their Binding Interactions with Human Serum Albumin.ACS omega · 2025Article
- Perspectives on NcRNAs in HBV/cccDNA-driven HCC progression.Cancer cell international · 2025Review
- A Dataset Curated for the Assessment of G4s in the LncRNAs Dysregulated in Various Human Cancers.Scientific data · 2025Article
- G-Quadruplex-Based Splice Switching as a Therapeutic Approach in Duchenne Muscular Dystrophy.ACS chemical biology · 2025Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear-retained long non-coding RNAs (lncRNAs) including MALAT1 have emerged as critical regulators of many molecular processes including transcription, alternative splicing and chromatin organization. Here, we report the presence of three conserved and thermodynamically stable RNA G-quadruplexes (rG4s) located in the 3' region of MALAT1. Using rG4 domain-specific RNA pull-down followed by mass spectrometry and RNA immunoprecipitation, we demonstrated that the MALAT1 rG4 structures are specifically bound by two nucleolar proteins, Nucleolin (NCL) and Nucleophosmin (NPM). Using imaging, we found that the MALAT1 rG4s facilitate the localization of both NCL and NPM to nuclear speckles, and specific G-to-A mutations that disrupt the rG4 structures compromised the localization of both NCL and NPM in speckles. In vitro biophysical studies established that a truncated version of NCL (ΔNCL) binds tightly to all three rG4s. Overall, our study revealed new rG4s within MALAT1, established that they are specifically recognized by NCL and NPM, and showed that disrupting the rG4s abolished localization of these proteins to nuclear speckles.
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