Journal
NATURE CHEMICAL BIOLOGY
Volume 6, Issue 8, Pages 610-614Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.405
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Funding
- Cancer Research Institute
- Anderson Cancer Center
- US National Institute of Allergy and Infectious Diseases of the US National Institutes of Health [AI041111, AI083284-01]
- Rockefeller University
- Ellison Medical Foundation
- Irma T. Hirschl and Monique Weill-Caulier Trust
- Lerner Trust
- US National Institute of Drug Abuse of the US National Institutes of Health [1R21DA025751-01]
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Identification of immune effectors and the post-translational modifications that control their activity is essential for dissecting mechanisms of immunity. Here we demonstrate that the antiviral activity of interferon-induced transmembrane protein 3 (IFITM3) is post-translationally regulated by S-palmitoylation. Large-scale profiling of palmitoylated proteins in a dendritic cell line using a chemical reporter strategy revealed over 150 lipid-modified proteins with diverse cellular functions, including innate immunity. We discovered that S-palmitoylation of IFITM3 on membrane-proximal cysteines controls its clustering in membrane compartments and its antiviral activity against influenza virus. The sites of S-palmitoylation are highly conserved among the IFITM family of proteins in vertebrates, which suggests that S-palmitoylation of these immune effectors may be an ancient post-translational modification that is crucial for host resistance to viral infections. The S-palmitoylation and clustering of IFITM3 will be important for elucidating its mechanism of action and for the design of antiviral therapeutics.
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