Abstract 1866 Proteome-wide screening for short linear docking motifs interacting with Saccharomyces cerevisiae MAP kinases

Mitogen-activated Protein Kinases (MAPKs) serve as important relay components in the eukaryotic cellular responses to a variety of critical extracellular cues. Canonical MAPKs act as the terminal members of an obligate 3-tiered kinase cascade. All MAPKs phosphorylate substrates within a conserved Ser/Thr-Pro sequence motif, and as such, catalytic site specificity cannot explain why each kinase targets a unique pool of substrates. Protein substrate specificity is provided through a second site, a distal docking groove that interacts with short linear sequence motifs found in unstructured regions of MAPK binding proteins.