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

tetano

Editor, Senior Moderator
J Virol. 2013 Jun 26. [Epub ahead of print]
Palmitoylation on conserved and non-conserved cysteines of murine IFITM1 regulates its stability and anti-influenza A virus activity.
Hach JC, McMichael T, Chesarino NM, Yount JS.
Source

Department of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, OH, 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 (m) IFITM1 is palmitoylated on one non-conserved cysteine and three conserved cysteines required for anti-influenza A virus activity. Additionally, palmitoylation of mIFITM1 regulates protein stability by preventing proteasomal degradation, and modification of the non-conserved cysteine at the mIFITM1 C-terminus supports an intramembrane topology with mechanistic implications.

PMID:
23804635
[PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/23804635
 
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