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Biochem Biophys Res Commun. 1994 Apr 29;200(2):1118-24.

The primary structure of a human MAP kinase activated protein kinase 2.

Author information

1
Department of Pathology, University of Connecticut Health Center, Farmington 06030.

Abstract

Mitogen-activated protein (MAP) kinase is of central importance in mediating intracellular actions in response to a variety of extracellular stimuli. MAP kinase activated protein (MAPKAP) kinase 2 is one of the two known protein kinases that can be phosphorylated and activated by MAP kinase. Here we present the first complete primary structure of MAPKAP kinase 2 elucidated from a human cDNA sequence. Sequence analysis reveals that MAPKAP kinase 2 is a 370 amino acid protein containing a proline-rich N-terminal region and a well conserved catalytic domain. Northern blot analysis of MAPKAP kinase 2 showed a 4.8 kb mRNA species in HL-60 cells. In addition, we also show the first evidence that recombinant MAPKAP kinase 2 is phosphorylated and activated by MAP kinase in vitro.

PMID:
8179591
DOI:
10.1006/bbrc.1994.1566
[Indexed for MEDLINE]

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