Work

Regulation of the Trafficking and Antiviral Activity of IFITM3 by Post-Translational Modifications

Year: 2014

Type: review

Abstract: 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.

Source: Future Microbiology

DOI: 10.2217/fmb.14.65

Authors: Nicholas M Chesarino, Temet M McMichael, Jacob S Yount

Institution: The Ohio State University

Language: English

Topic: interferon and immune responses

Subfield: Immunology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funders: American Society for Microbiology, National Institutes of Health, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases