ArticleJournal of virology2013
Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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
32 citing papers in PubMed, 46 citations in OpenAlex.
- Stress granules at the crossroads of retroviral replication and antiviral immunity: mechanisms and therapeutic opportunities.Molecular biology reports · 2026Review
- Mechanisms of APOBEC3 Packaging into HIV-1.Viruses · 2026Review
- Guardian ubiquitin E3 ligases target cancer-associated APOBEC3 deaminases for degradation to promote human genome integrity.Nature communications · 2026Article
- APOBEC3B drives PKR-mediated translation shutdown and protects stress granules in response to viral infection.Nature communications · 2023Article
- The SARS-CoV-2 targeted human RNA binding proteins network biology to investigate COVID-19 associated manifestations.International journal of biological macromolecules · 2022Article
- Unwinding the roles of RNA helicase MOV10.Wiley interdisciplinary reviews. RNA · 2022Review
- Highly-potent, synthetic APOBEC3s restrict HIV-1 through deamination-independent mechanisms.PLoS pathogens · 2021Article
- Noncanonical Functions and Cellular Dynamics of the Mammalian Signal Recognition Particle Components.Frontiers in molecular biosciences · 2021Review
- Host restriction of emerging high-pathogenic bunyaviruses via MOV10 by targeting viral nucleoprotein and blocking ribonucleoprotein assembly.PLoS pathogens · 2020Article
- Effect of P-body component Mov10 on HCV virus production and infectivity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- EXOSC9 depletion attenuates P-body formation, stress resistance, and tumorigenicity of cancer cells.Scientific reports · 2020Article
- The MOV10 helicase restricts hepatitis B virus replication by inhibiting viral reverse transcription.The Journal of biological chemistry · 2019Article
- The Role of RNA in HIV-1 Vif-Mediated Degradation of APOBEC3H.Journal of molecular biology · 2019Article
- Effects of Moloney Leukemia Virus 10 Protein on Hepatitis B Virus Infection and Viral Replication.Viruses · 2019Article
- Viral Regulation of RNA Granules in Infected Cells.Virologica Sinica · 2019Review
- Structural Determinants of the APOBEC3G N-Terminal Domain for HIV-1 RNA Association.Frontiers in cellular and infection microbiology · 2019Article
- APOBEC3H Subcellular Localization Determinants Define Zipcode for Targeting HIV-1 for Restriction.Molecular and cellular biology · 2018Article
- Formation of RNA Granule-Derived Capsid Assembly Intermediates Appears To Be Conserved between Human Immunodeficiency Virus Type 1 and the Nonprimate Lentivirus Feline Immunodeficiency Virus.Journal of virology · 2018Article
- The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism.Molecular cell · 2018Article
- Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin-proteasome pathway.Retrovirology · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Mov10 and APOBEC3G (A3G) localize to cytoplasmic granules called processing bodies (P bodies), incorporate into human immunodeficiency virus type 1 (HIV-1) virions, and inhibit viral replication. The functional relevance of Mov10/A3G P-body localization to virion incorporation and antiviral activity has not been fully explored. We found that a helicase V mutant of Mov10 exhibits significantly reduced localization to P bodies but still efficiently inhibits viral infectivity via virion incorporation. Disruption of the P bodies by DDX6 knockdown also confirmed Mov10 antiviral activity without P-body localization. In addition, overexpression of SRP19, which binds to 7SL RNA, depleted A3G from P bodies but did not affect its virion incorporation. Sucrose gradient sedimentation assays revealed that the majority of Mov10, A3G, HIV-1 RNA, and Gag formed high-molecular-mass (HMM) complexes that are converted to low-molecular-mass (LMM) complexes after RNase A treatment. In contrast, the P-body markers DCP2, LSM1, eIF4e, DDX6, and AGO1 were in LMM complexes, whereas AGO2, an effector protein of the RNA-induced silencing complex that localizes to P bodies, was present in both LMM and HMM complexes. Depletion of AGO2 indicated that RNA-induced silencing function is required for Mov10's ability to reduce Gag expression upon overexpression, but not its virion incorporation or effect on virus infectivity. We conclude that the majority of Mov10 and A3G are in HMM complexes, whereas most of the P-body markers are in LMM complexes, and that virion incorporation and the antiviral activities of Mov10 and A3G do not require their localization to P bodies.
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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.