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Palmitoylome profiling reveals S-palmitoylation–dependent antiviral activity of IFITM3.
- Source :
-
Nature Chemical Biology . Aug2010, Vol. 6 Issue 8, p610-614. 5p. 1 Color Photograph, 3 Graphs. - Publication Year :
- 2010
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- *DENDRITIC cells
*CELL lines
*NATURAL immunity
*PROTEINS
*ANTIVIRAL agents
Subjects
Details
- Language :
- English
- ISSN :
- 15524450
- Volume :
- 6
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Nature Chemical Biology
- Publication Type :
- Academic Journal
- Accession number :
- 52303073
- Full Text :
- https://doi.org/10.1038/nchembio.405