Early activation of the cell signaling protein, focal adhesion kinase (FAK) upon equine herpesvirus type 1 (EHV-1) infection.
Presentation
Overview
Overview
Description
To productively infect cells, equine herpesvirus type 1 (EHV-1) triggers specific cell signal transduction pathways. Previous work by our group showed that the cellular, serine/threonine, Rho kinase, ROCK1 is activated very early upon EHV-1 infection and that this activation is critical for virus infection. In the current study we investigated which cell signaling molecules are activated by ROCK1 after EHV-1 infection. To examine the role of specific ROCK1-associated cellular proteins in EHV-1 infection, the phosphorylation of downstream targets of ROCK1 were evaluated by western blotting using phospho-specific antibodies against proteins that are known to be actively phosphorylated directly or indirectly by ROCK1 in other systems, including the ezrin/radixin/moesin complex (ERM), LIMK1/2, and focal adhesion kinase (FAK). Our data show that FAK is phosphorylated as early as 15 minutes after infection, while LIMK1/2 and erm are not phosphorylated. In addition, the inhibition of FAK phosphorylation in the presence of a ROCK1 inhibitor indicates that FAK is downstream of ROCK1 in the signal transduction pathway. Further studies are underway to 1) identify other cell signaling molecules that are activated upon EHV-1 infection and 2) to unravel how these cellular proteins contribute to EHV-1 infection.
