The Primary Structure of a Human Map Kinase Activated Protein Kinase 2 Academic Article Article uri icon

Overview

MeSH Major

  • Animal Experimentation
  • Attitude of Health Personnel
  • Biomedical Research
  • Research Personnel
  • Terrorism

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.

publication date

  • April 30, 1994

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1994.1566

PubMed ID

  • 8179591

Additional Document Info

start page

  • 1118

end page

  • 24

volume

  • 200

number

  • 2