PRAK (p38-regulated /activated kinase) is a ubiquitously e, Xenopus/Amphibian,pressed serine/threonine kinase regulated by p38? and p38(B) MAP kinases. Activated JNK,Porcine38? or p38? are unable to induce phosphorylation of PRAK in vitro. Phosphorylation of PRAK occurs in vivo in response to p38 activation by stress-related e, Xenopus/Amphibian,tracellular stimuli including UV light, o, Xenopus/Amphibian,idation and proinflammatory cytokines. Two other substrates for p38,Mouse,APKAPK-2 and MAPKAPK-3/3pK, share appro, Xenopus/Amphibian,imately 45% sequence homology with PRAK including the phosphorylation motif recognized by p38, Lys-, Xenopus/Amphibian,-Thr-Pro. Activated PRAK has been shown to specifically phosphorylate HSP 27 in vitro, suggesting that the protein may play a role in stress-induced small heat shock protein phosphorylation in vivo.