Journal
JOURNAL OF VIROLOGY
Volume 87, Issue 17, Pages 9923-9927Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00621-13
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Funding
- NIH/NIAID [AI095348]
- Ohio State University
- Ohio State University Systems and Integrative Biology Training Program
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The interferon-induced transmembrane proteins (IFITMs) restrict infection by numerous viruses, yet the importance and regulation of individual isoforms remains unclear. Here, we report that murine IFITM1 (mIFITM1) is palmitoylated on one nonconserved cysteine and three conserved cysteines that are required for anti-influenza A virus activity. Additionally, palmitoylation of mIFITM1 regulates protein stability by preventing proteasomal degradation, and modification of the nonconserved cysteine at the mIFITM1 C terminus supports an intramembrane topology with mechanistic implications.
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