期刊
FUTURE MICROBIOLOGY
卷 9, 期 10, 页码 1151-1163出版社
FUTURE MEDICINE LTD
DOI: 10.2217/FMB.14.65
关键词
antiviral; IFITM3; intramembrane domain; methylation; palmitoylation; phosphorylation; post-translational modification; ubiquitination
类别
资金
- NIH/NIAID [R00AI095348]
- Ohio State University Public Health Preparedness for Infectious Diseases program
- Ohio State University Systems and Integrative Biology Training Program (NIH/NIGMS) [T32GM068412]
- American Society for Microbiology
IFITM3 restricts cellular infection by multiple important viral pathogens, and is particularly critical for the innate immune response against influenza virus. Expression of IFITM3 expands acidic endolysosomal compartments and prevents fusion of endocytosed viruses, leading to their degradation. This small, 133 amino acid, antiviral protein is controlled by at least four distinct post-translational modifications. Positive regulation of IFITM3 antiviral activity is provided by S-palmitoylation, while negative regulatory mechanisms include lysine ubiquitination, lysine methylation and tyrosine phosphorylation. Herein, we describe specific insights into IFITM3 trafficking and activity that were provided by studies of IFITM3 post-translational modifications, and discuss evidence suggesting that IFITM3 adopts multiple membrane topologies involving at least one intramembrane domain in its antivirally active conformation.
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