Palmitoylation on Conserved and Nonconserved Cysteines of Murine IFITM1 Regulates Its Stability and Anti-Influenza A Virus Activity

被引：67

作者：

Hach, Jocelyn C. ^{[1
]}

McMichael, Temet ^{[1
]}

Chesarino, Nicholas M. ^{[1
]}

Yount, Jacob S. ^{[1
]}

机构：

[1] Ohio State Univ, Dept Microbial Infect & Immun, Ctr Microbial Interface Biol, Columbus, OH 43210 USA

来源：

JOURNAL OF VIROLOGY | 2013年 / 87卷 / 17期

关键词：

S-ACYLTRANSFERASES; ANTIVIRAL ACTIVITY; PROTEINS; LOCALIZATION; INFLUENZA; RESISTANCE; ENZYMES; FAMILY;

D O I：

10.1128/JVI.00621-13

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：9923 / 9927

页数：5

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