Overview:

MAPKAPK5 is a member of the serine/threonine kinase family that responds to cellular stress and proinflammatory cytokines. MAPKAPK5 is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta (1). MAPKAPK5 is activated in HeLa cells in response to cellular stress and proinflammatory cytokines. MAPKAPK5 activity is regulated by p38-alpha and p38-beta both in vitro and in vivo, and thr-182 is the regulatory phosphorylation site of MAPKAPK5 (2). In vitro, MAPKAPK5 kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites.

Gene Aliases:

PRAK

Genbank Number:

NM_003668

References:

1. New, L.; Jiang, Y. et al: PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J. 17: 3372-3384, 1998.

2. Ni, H.; Wang. et al: MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase. Biochem. Biophys. Res. Commun. 243: 492-496, 1998.