ArticleScientific reports2017
Direct binding to GABARAP family members is essential for HIV-1 Nef plasma membrane localization.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- GABARAP proteins regulate the packaging of HIV-1 genomic RNA into virions.EMBO reports · 2025Article
- Profiling HIV1-host protein-protein interaction networks in patient-derived exosome proteins: impact on pathophysiology and innate immune pathways.Virology journal · 2025Article
- HIV protein Nef expression in human microglia drives the release of distinct Nef-containing extracellular vesicles.Extracellular vesicles and circulating nucleic acids · 2025Article
- Identification of the GABARAP binding determinant in PI4K2A.Bioscience reports · 2024Article
- A new perspective on the autophagic and non-autophagic functions of the GABARAP protein family: a potential therapeutic target for human diseases.Molecular and cellular biochemistry · 2024Review
- TBK1 and GABARAP family members suppress Coxsackievirus B infection by limiting viral production and promoting autophagic degradation of viral extracellular vesicles.PLoS pathogens · 2022Article
- Does GEC1 Enhance Expression and Forward Trafficking of the Kappa Opioid Receptor (KOR) via Its Ability to Interact with NSF Directly?Handbook of experimental pharmacology · 2022Article
- The interplay between pathogens and Atg8 family proteins: thousand-faced interactions.FEBS open bio · 2021Review
- Automated machine learning optimizes and accelerates predictive modeling from COVID-19 high throughput datasets.Scientific reports · 2021Article
- Extracellular vesicles in virus infection and pathogenesis.Current opinion in virology · 2020Review
- Deficiency of GABARAP but not its Paralogs Causes Enhanced EGF-induced EGFR Degradation.Cells · 2020Article
- Human LC3 and GABARAP subfamily members achieve functional specificity via specific structural modulations.Autophagy · 2020Article
- Human ubiquitin-like proteins as central coordinators in autophagy.Interface focus · 2018Article
- Comobility of GABARAP and Phosphatidylinositol 4-Kinase 2A on Cytoplasmic Vesicles.Biochemistry · 2018Article
- The Atg8 Family of Proteins-Modulating Shape and Functionality of Autophagic Membranes.Frontiers in genetics · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HIV-1 Nef is an important pathogenic factor for HIV/AIDS pathogenesis. Studies have shown that the association of Nef with the inner leaflet of the plasma membrane and with endocytic and perinuclear vesicles is essential for most activities of Nef. Using purified recombinant proteins in pull-down assays and by co-immunoprecipitation assays we demonstrate that Nef binds directly and specifically to all GABARAP family members, but not to LC3 family members. Based on nuclear magnetic resonance (NMR) experiments we showed that Nef binds to GABARAP via two surface exposed hydrophobic pockets. S53 and F62 of GABARAP were identified as key residues for the interaction with Nef. During live-cell fluorescence microscopy an accumulation of Nef and all GABARAP family members in vesicular structures throughout the cytoplasm and at the plasma membrane was observed. This plasma membrane accumulation was significantly reduced after knocking down GABARAP, GABARAPL1 and GABARAPL2 with respective siRNAs. We identified GABARAPs as the first known direct interaction partners of Nef that are essential for its plasma membrane localization.
Indexed as
Identifiers
What OpenQuestion holds
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.