MAP kinase phosphatases

Genome Biol. 2002 Jun 26;3(7):REVIEWS3009. doi: 10.1186/gb-2002-3-7-reviews3009. Epub 2002 Jun 26.

Abstract

Mitogen-activated protein MAP kinases are key signal-transducing enzymes that are activated by a wide range of extracellular stimuli. They are responsible for the induction of a number of cellular responses, such as changes in gene expression, proliferation, differentiation, cell cycle arrest and apoptosis. Although regulation of MAP kinases by a phosphorylation cascade has long been recognized as significant, their inactivation through the action of specific phosphatases has been less studied. An emerging family of structurally distinct dual-specificity serine, threonine and tyrosine phosphatases that act on MAP kinases consists of ten members in mammals, and members have been found in animals, plants and yeast. Three subgroups have been identified that differ in exon structure, sequence and substrate specificity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Catalytic Domain
  • Evolution, Molecular
  • Mitogen-Activated Protein Kinases / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoprotein Phosphatases* / chemistry
  • Phosphoprotein Phosphatases* / classification
  • Phosphoprotein Phosphatases* / genetics
  • Phosphoprotein Phosphatases* / physiology
  • Phylogeny
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Substrate Specificity

Substances

  • Mitogen-Activated Protein Kinases
  • Phosphoprotein Phosphatases