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 Rho kinase, ROCK1, is activated 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. Our data show that focal adhesion kinase (FAK) is phosphorylated as early as 15 minutes after infection. In addition, FAK phosphoryl;ation is blocked in the presence of a ROCK1 inhibitor indicating that FAK is downstream of ROCK1 in the signal transduction pathway.
