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

Rebecca A Bozym1, Elizabeth Delorme-Axford, Katharine Harris

  • 1Department of Microbiology and Molecular Genetics, University of Pittsburgh, Pittsburgh, PA 15219, USA.

Cell Host & Microbe
|February 21, 2012
PubMed

Insights

Focal adhesion kinase (FAK) links viral actin cytoskeleton changes to innate immune signaling by activating MAVS. Enteroviruses cleave FAK, suppressing this antiviral response.

Area of Science:

  • Virology
  • Immunology
  • Cell Biology

Background:

  • Viruses manipulate the host actin cytoskeleton during infection.
  • Cellular detection of cytoskeletal alterations may be crucial for recognizing viral infections.
  • Focal adhesion kinase (FAK) is a key signaling molecule in cellular processes.

Purpose of the Study:

  • To investigate the role of FAK in antiviral innate immune signaling.
  • To determine how FAK interacts with antiviral signaling pathways.
  • To understand how viruses might evade FAK-mediated antiviral responses.

Main Methods:

  • Utilized FAK-deficient cells to assess susceptibility to viral infection.
  • Investigated FAK interaction with mitochondrial antiviral signaling adaptor (MAVS) during infection.
  • Examined the effect of viral protease activity on FAK function.

Main Results:

  • FAK-deficient cells exhibit increased susceptibility to RNA virus infection and impaired antiviral signaling.
  • FAK interacts with MAVS at the mitochondrial membrane in a virus-dependent manner.
  • FAK potentiates MAVS signaling independently of its kinase activity.
  • Enterovirus cysteine proteases cleave FAK, inhibiting its innate immune signaling role.

Conclusions:

  • FAK acts as a crucial component of the RIG-I-like receptor antiviral signaling pathway.
  • FAK bridges the sensing of virus-induced cytoskeletal changes to MAVS activation.
  • Viral manipulation of FAK is a mechanism to suppress innate antiviral immunity.

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