Focal adhesion kinase is a component of antiviral RIG-I-like receptor signaling.

Bozym RA, Delorme-Axford E, Harris K, Morosky S, Ikizler M, Dermody TS, Sarkar SN, Coyne CB
Cell Host Microbe. 2012 11 (2): 153-66

PMID: 22341464 · PMCID: PMC3995454 · DOI:10.1016/j.chom.2012.01.008

Viruses modulate the actin cytoskeleton at almost every step of their cellular journey from entry to egress. Cellular sensing of these cytoskeletal changes may function in the recognition of viral infection. Here we show that focal adhesion kinase (FAK), a focal adhesion localized tyrosine kinase that transmits signals between the extracellular matrix and the cytoplasm, serves as a RIG-I-like receptor antiviral signaling component by directing mitochondrial antiviral signaling adaptor (MAVS) activation. Cells deficient in FAK are highly susceptible to RNA virus infection and attenuated in antiviral signaling. We show that FAK interacts with MAVS at the mitochondrial membrane in a virus infection-dependent manner and potentiates MAVS-mediated signaling via a kinase-independent mechanism. A cysteine protease encoded by enteroviruses cleaves FAK to suppress its role in innate immune signaling. These findings suggest that FAK serves as a link between cytoskeletal perturbations that occur during virus infection and activation of innate immune signaling.

Copyright © 2012 Elsevier Inc. All rights reserved.

MeSH Terms (9)

Adaptor Proteins, Signal Transducing Cell Line Focal Adhesion Protein-Tyrosine Kinases Humans Mitochondrial Membranes Protein Interaction Mapping RNA Viruses Signal Transduction Viral Plaque Assay

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