ArticlemBio2022
ABHD16A Negatively Regulates the Palmitoylation and Antiviral Function of IFITM Proteins.
Article in mBio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 22 citations in OpenAlex.
- The role of protein palmitoylation in disease pathogenesis and therapeutic innovation.Annals of medicine · 2026Review
- Emerging roles of α/β hydrolase domain (ABHD) proteins in S-palmitoylation modification: molecular mechanisms, structural features, and pathological implications.Cellular & molecular biology letters · 2026Review
- The Phospholipase AJournal of lipid and atherosclerosis · 2026Review
- Review
- Distribution and influence of single-nucleotide polymorphisms affecting bovine leukemia virus proviral load in semen and progeny derived from semen in Japanese Black cattle.The Journal of veterinary medical science · 2026Article
- IFITM3 at the viral fusion-pore checkpoint: membrane energetics and entry-route-dependent outcomes.Frontiers in immunology · 2026Review
- Multi-Omics Characterization of ABHD12 Across Pan-Cancer and Validation of Its Role in Promoting Proliferation and Metastasis in Breast Cancer.Breast cancer (Dove Medical Press) · 2026Article
- S-palmitoylation and depalmitoylation at the interface of animal virus-host interactions.Frontiers in cellular and infection microbiology · 2026Review
- The function and mechanism of protein acylation in the regulation of viral infection.Virulence · 2025Review
- Recent advances in S-palmitoylation and its emerging roles in human diseases.Journal of hematology & oncology · 2025Review
- The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A.Biomolecules · 2025Article
- Depalmitoylase ABHD16A negatively regulates the anti-hepatitis B virus activity of IFITM1.Microbiology spectrum · 2025Article
- Review
- Swine RNF5 positively regulates the antiviral activity of IFITM1 by mediating the degradation of ABHD16A.Journal of virology · 2025Article
- The CP123L protein of African swine fever virus is a membrane-associated, palmitoylated protein required for viral replication.Journal of virology · 2025Article
- Pooled PPIseq: Screening the SARS-CoV-2 and human interface with a scalable multiplexed protein-protein interaction assay platform.PloS one · 2025Article
- From Classical to Alternative Pathways of 2-Arachidonoylglycerol Synthesis: AlterAGs at the Crossroad of Endocannabinoid and Lysophospholipid Signaling.Molecules (Basel, Switzerland) · 2024Review
- The Antiviral Activity of Interferon-Induced Transmembrane Proteins and Virus Evasion Strategies.Viruses · 2024Review
- Discovery and Characterization of IFITMViruses · 2023Review
- Mechanisms of Modulation of Mitochondrial Architecture.Biomolecules · 2023Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interferon-inducible transmembrane (IFITM) proteins are small homologous proteins that are encoded by the interferon-stimulated genes (ISGs), which can be strongly induced by interferon (IFN) and provide resistance to invasion by a variety of viral pathogens. However, the exact molecular mechanisms underlying this function have remained elusive. The antiviral activity of IFITMs from different species depends on S-palmitoylation at conserved cysteine residues. However, specific enzymes involved in the dynamic palmitoylation cycle of IFITMs, especially depalmitoylase, have not yet been reported. Here, we demonstrate that α/-hydrolase domain-containing 16A (ABHD16A) is a depalmitoylase and a negative regulator of IFITM protein that can catalyze the depalmitoyl reaction of S-palmitoylated IFITM proteins, thereby decreasing their antiviral activities on RNA viruses. Using the acyl-PEGyl exchange gel shift (APEGS) assay, we identified ABHD16A proteins from humans, pigs, and mice that can directly participate in the palmitoylation/depalmitoylation cycles of IFITMs in the constructed
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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.