ArticleJournal of immunology (Baltimore, Md. : 1950)2011
Polypyrimidine tract-binding protein is critical for the turnover and subcellular distribution of CD40 ligand mRNA in CD4+ T cells.
Article in Journal of immunology (Baltimore, Md. : 1950), 2011. 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, 21 citations in OpenAlex.
- PTBP1 and Cancer: From RNA Regulation to Therapeutic Potential.Journal of cellular and molecular medicine · 2025Review
- Celastrus orbiculatus extract suppresses gastric cancer stem cells through the TGF-β/Smad signaling pathway.Journal of natural medicines · 2024Article
- Long noncoding RNA SGO1-AS1 inactivates TGFβ signaling by facilitating TGFB1/2 mRNA decay and inhibits gastric carcinoma metastasis.Journal of experimental & clinical cancer research : CR · 2021Article
- A Posttranscriptional Pathway of CD40 Ligand mRNA Stability Is Required for the Development of an Optimal Humoral Immune Response.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Identification and Characterization of a Minimal Functional Splicing Regulatory Protein, PTBP1.Biochemistry · 2020Article
- CRISPR/Cas9 Screens Reveal Multiple Layers of B cell CD40 Regulation.Cell reports · 2019Article
- Mammalian RNA switches: Molecular rheostats in gene regulation, disease, and medicine.Computational and structural biotechnology journal · 2019Review
- Long non-coding RNA-dependent mechanism to regulate heme biosynthesis and erythrocyte development.Nature communications · 2018Article
- PTBP1 modulation of MCL1 expression regulates cellular apoptosis induced by antitubulin chemotherapeutics.Cell death and differentiation · 2016Article
- CD5 expression is regulated during human T-cell activation by alternative polyadenylation, PTBP1, and miR-204.European journal of immunology · 2016Article
- The RNA-Binding Protein, Polypyrimidine Tract-Binding Protein 1 (PTBP1) Is a Key Regulator of CD4 T Cell Activation.PloS one · 2016Article
- Experimental Neuromyelitis Optica Induces a Type I Interferon Signature in the Spinal Cord.PloS one · 2016Article
- Article
- New insights into functional roles of the polypyrimidine tract-binding protein.International journal of molecular sciences · 2013Review
- Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2.Critical reviews in biochemistry and molecular biologyArticle
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
CD40L (CD154) is regulated at the posttranscriptional level by an activation-induced process that results in a highly stable transcript at extended times of T cell activation. Transcript stability is mediated by polypyrimidine tract-binding protein (PTB)-containing complexes (complex I and II) that bind to three adjacent CU-rich sequences within the 3' untranslated region. To assess the role of PTB in the expression and distribution of CD40L mRNA, PTB was targeted using short hairpin RNA in both primary T cells and a T cell line that recapitulates the stability phase of regulated CD40L mRNA decay. PTB knockdown resulted in a marked decrease in the mRNA stability that resulted in lowered CD40L surface expression. PTB was also critical for appropriate distribution of CD40L mRNA between the nucleus and cytoplasm and in the cytoplasm between the cytosol and the translating polysomes. The activation-induced formation of PTB-specific ribonucleoprotein complexes was observed only with cytoplasmic and not nuclear PTB indicating functional differences in the protein defined by cellular localization. Finally, we observed that cytoplasmic and nuclear PTB isoforms were differentially modified relative to each other and that the changes in cytoplasmic PTB were consistent with activation-induced phosphorylation. Together this work suggests that differentially modified PTB regulates CD40L expression at multiple steps by 1) retaining CD40L mRNA in the nucleus, 2) directly regulating mRNA stability at late times of activation, and 3) forming a ribonuclear complex that preferentially associates with translating ribosomes thus leading to an enhanced level of CD40L protein.
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