The Primary Structure of a Human Map Kinase Activated Protein Kinase 2

You Li Zu, Fengying Y. Wu, Annette Gilchrist, Youxi X. Ai, Mark E. Labadia, Chi Kuang Huang

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1118-1124
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - 1994

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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