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Biochem Biophys Res Commun. 1998 Feb 13;243(2):492-6.

MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase.

Author information

1
Department of Chemistry, University of North Carolina, Chapel Hill 27599, USA.

Abstract

A novel protein kinase that has significant sequence homology to mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK) was identified. This novel protein kinase has a nucleotide sequence that encodes a protein of 473 amino acids and shares 45%, 46%, and 44% amino acid sequence identities to MAPKAPK2, 3 and 4 respectively. Northern blot analysis revealed that it has a wide tissue distribution. This novel protein kinase designated MAPKAPK5 can be phosphorylated by extracellular-regulated kinase (ERK), and p38 kinase but not by c-jun N-terminal kinase (JNK) in vitro. Recombinant GST-MAPKAPK5 protein can phosphorylate a peptide derived from the regulatory light chain of myosin II. Phosphorylation of MAPKAPK5 by ERK and p38 kinase increased its activity by 9 and 15 fold respectively. Taken together, these data suggest that MAPKAPK5 is a novel in vitro substrate for ERK and p38 kinase.

PMID:
9480836
DOI:
10.1006/bbrc.1998.8135
[Indexed for MEDLINE]

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