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J Virol. 2013 Sep;87(17):9923-7. doi: 10.1128/JVI.00621-13. Epub 2013 Jun 26.

Palmitoylation on conserved and nonconserved cysteines of murine IFITM1 regulates its stability and anti-influenza A virus activity.

Author information

1
Department of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, Ohio, USA.

Abstract

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.

PMID:
23804635
PMCID:
PMC3754091
DOI:
10.1128/JVI.00621-13
[Indexed for MEDLINE]
Free PMC Article

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