棕榈酰化作用于保守和非保守半胱氨酸的鼠干扰素诱导跨膜蛋白 1 调节其稳定性和抗甲型流感病毒活性。
Palmitoylation on conserved and nonconserved cysteines of murine IFITM1 regulates its stability and anti-influenza A virus activity.
机构信息
Department of Microbial Infection and Immunity, Center for Microbial Interface Biology, The Ohio State University, Columbus, Ohio, USA.
出版信息
J Virol. 2013 Sep;87(17):9923-7. doi: 10.1128/JVI.00621-13. Epub 2013 Jun 26.
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.
摘要
干扰素诱导跨膜蛋白（IFITMs）限制了多种病毒的感染，但各个亚型的重要性和调节仍不清楚。在这里，我们报告说，鼠源 IFITM1（mIFITM1）在一个非保守半胱氨酸和三个保守半胱氨酸上发生棕榈酰化，这些半胱氨酸对于抗甲型流感病毒活性是必需的。此外，mIFITM1 的棕榈酰化通过防止蛋白酶体降解来调节蛋白质稳定性，并且 mIFITM1 C 末端非保守半胱氨酸的修饰支持具有机械意义的跨膜拓扑结构。
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