Comparative studies of a new subfamily of human Ste20-like kinases: Homodimerization, subcellular localization, and selective activation of MKK3 and p38

J.T. Yustein, L. Xia, J.M. Kahlenburg, D. Robinson, D. Templeton, H.-J. Kung

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

The Sterile-20 or Ste20 family of serine/threonine kinases is a group of signaling molecules whose physiological roles within mammalian cells are just starting to be elucidated. Here, in this report we present the characterization of three human Ste20-like kinases with greater than 90% similarity within their catalytic domains that define a novel subfamily of Ste20s. Members of this kinase family include rat thousand and one (TAO1) and chicken KFC (kinase from chicken). For the lack of a consensus nomenclature in the literature, in this report, we shall call this family hKFC (for their homology to chicken KFC) and the three members hKFC-A, hKFC-B, and hKFC-C, respectively. These kinases have many similarities including an aminoterminal kinase domain, a serine-rich region, and a coiled-coil configuration within the C-terminus. All three kinases are able to activate the p38 MAP kinase pathway through the specific activation of the upstream MKK3 kinase. We also offer evidence, both theoretical and biochemical, showing that these kinases can undergo self-association. Despite these similarities, these kinases differ in tissue distribution, apparent subcellular localization, and feature structural differences largely within the carboxyl-terminal sequence.
Original languageEnglish
Pages (from-to)6129-6141
Number of pages13
JournalOncogene
Volume22
Issue number40
DOIs
Publication statusPublished - 2003
Externally publishedYes

Keywords

  • p38 MAPK
  • Ste20 kinase
  • TAO
  • mitogen activated protein kinase
  • protein serine threonine kinase
  • sterile 20 kinase
  • unclassified drug
  • amino terminal sequence
  • article
  • carboxy terminal sequence
  • cellular distribution
  • controlled study
  • dimerization
  • enzyme activation
  • enzyme phosphorylation
  • human
  • human cell
  • nonhuman
  • nucleotide sequence
  • priority journal
  • protein domain
  • protein family
  • sequence homology
  • signal transduction
  • tissue distribution
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cercopithecus aethiops
  • COS Cells
  • Dimerization
  • Gene Expression Regulation, Enzymologic
  • Humans
  • Isoenzymes
  • Jurkat Cells
  • Male
  • MAP Kinase Kinase 3
  • Mitogen-Activated Protein Kinase Kinases
  • Mitogen-Activated Protein Kinases
  • Molecular Sequence Data
  • p38 Mitogen-Activated Protein Kinases
  • Phylogeny
  • Protein Conformation
  • Protein-Serine-Threonine Kinases
  • Protein-Tyrosine Kinases
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
  • Subcellular Fractions
  • Tissue Distribution
  • Gallus gallus
  • Mammalia

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