ArticleNucleic acids research2016
B'-protein phosphatase 2A is a functional binding partner of delta-retroviral integrase.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 35 citations in OpenAlex.
- The Host Cell Factor Phosphatase-2A Subunit PR130 Restricts Replication of Herpes Simplex Virus Type-1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Single-cell delineation of strain-specific HIV-1 Vif activities using dual reporter sensor cells and live cell imaging.Journal of virology · 2025Article
- Structural insights into PPP2R5A degradation by HIV-1 Vif.Nature structural & molecular biology · 2024Article
- Brief Histories of Retroviral Integration Research and Associated International Conferences.Viruses · 2024Review
- Review
- Evolutionary Conservation of PP2A Antagonism and G2/M Cell Cycle Arrest in Maedi-Visna Virus Vif.Viruses · 2022Article
- Role of miRNAs in Human T Cell Leukemia Virus Type 1 Induced T Cell Leukemia: A Literature Review and Bioinformatics Approach.International journal of molecular sciences · 2022Review
- Structure and function of retroviral integrase.Nature reviews. Microbiology · 2022Review
- Current Perspectives in Human T-Cell Leukemia Virus Type 1 Infection and Its Associated Diseases.Frontiers in medicine · 2022Review
- Structural basis for the inhibition of HTLV-1 integration inferred from cryo-EM deltaretroviral intasome structures.Nature communications · 2021Article
- PP2A Phosphatase as an Emerging Viral Host Factor.Frontiers in cellular and infection microbiology · 2021Review
- Strategies for Targeting Retroviral Integration for Safer Gene Therapy: Advances and Challenges.Frontiers in molecular biosciences · 2021Review
- Retroviral integrase: Structure, mechanism, and inhibition.The Enzymes · 2021Article
- Functional and Structural Insights into a Vif/PPP2R5 Complex Elucidated Using Patient HIV-1 Isolates and Computational Modeling.Journal of virology · 2020Article
- Cryo-EM structure of the deltaretroviral intasome in complex with the PP2A regulatory subunit B56γ.Nature communications · 2020Article
- Structural basis of host protein hijacking in human T-cell leukemia virus integration.Nature communications · 2020Article
- Dual Functionality of HIV-1 Vif in APOBEC3 Counteraction and Cell Cycle Arrest.Frontiers in microbiology · 2020Review
- Inhibition of HTLV-1 Infection by HIV-1 First- and Second-Generation Integrase Strand Transfer Inhibitors.Frontiers in microbiology · 2019Article
- Joint ancestry and association test indicate two distinct pathogenic pathways involved in classical dengue fever and dengue shock syndrome.PLoS neglected tropical diseases · 2018Article
- HTLV-1: Regulating the Balance Between Proviral Latency and Reactivation.Frontiers in microbiology · 2018Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
To establish infection, a retrovirus must insert a DNA copy of its RNA genome into host chromatin. This reaction is catalysed by the virally encoded enzyme integrase (IN) and is facilitated by viral genus-specific host factors. Herein, cellular serine/threonine protein phosphatase 2A (PP2A) is identified as a functional IN binding partner exclusive to δ-retroviruses, including human T cell lymphotropic virus type 1 and 2 (HTLV-1 and HTLV-2) and bovine leukaemia virus (BLV). PP2A is a heterotrimer composed of a scaffold, catalytic and one of any of four families of regulatory subunits, and the interaction is specific to the B' family of the regulatory subunits. B'-PP2A and HTLV-1 IN display nuclear co-localization, and the B' subunit stimulates concerted strand transfer activity of δ-retroviral INs in vitro. The protein-protein interaction interface maps to a patch of highly conserved residues on B', which when mutated render B' incapable of binding to and stimulating HTLV-1 and -2 IN strand transfer activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.