Abstract

So-called proline-directed kinases phosphorylate a Ser/Thr residue preceding a Pro residue. This low specificity site is recognised by a large family of MAP and CDK-like kinases. However, the kinases achieve their target substrate specificity through separate docking motifs which are also required to activate the kinase enzymatic function. A docking motif should be present in a candidate substrate sequence - or any (S/T)P motifs are unlikely to be meaningful. For example the P38 MAP kinase is activated by motifs approximating to (R/K)XXXX#X# where # is a hydrophobic residue (Chang et al. (2002) 12086621) and ERK kinase is also activated by FxFP-like motifs (Fantz et al. (2001) 11371562).