MAP kinase phosphatases.

Aspasia Theodosiou; Alan Ashworth

doi:10.1186/gb-2002-3-7-reviews3009

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MAP kinase phosphatases.

Aspasia Theodosiou·Alan Ashworth

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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.

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Amino Acid Sequence Animals Binding Sites Catalytic Domain Evolution, Molecular Mitogen-Activated Protein Kinases Models, Molecular Molecular Sequence Data Phosphoprotein Phosphatases Phylogeny Protein Structure, Tertiary Sequence Alignment Substrate Specificity Journal Article Research Support, Non-U.S. Gov't Review

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Aspasia Theodosiou, Alan Ashworth. 2002-06-26. MAP kinase phosphatases.. https://doi.org/10.1186/gb-2002-3-7-reviews3009

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