The stress-activated MAPK Hog1 in Cochliobolus heterostrophus, a maize foliar pathogen, undergoes dephosphorylation upon exposure to ferulic acid (FA), a phenolic compound abundant in the host plant. Unlike its nuclear localization during osmotic stress, Hog1:GFP forms cytoplasmic foci in response to FA, indicating its sequestering. By using Hog1:GFP as an affinity purification bait, we isolated an FA-dependent sub-proteome from a subcellular fraction enriched with fluorescent foci. The identified proteins include RNA-binding proteins, translation initiation factors and mitochondrial proteins, suggesting the foci to be stress granules.