Protein family review

MAP kinase phosphatases

Aspasia Theodosiou¹ and Alan Ashworth²

¹Biomedical Sciences Research Centre 'Alexander Fleming', PO Box 74145, Varkiza 166-02, Athens, Greece

²The Breakthrough Breast Cancer Research Centre, Institute of Cancer Research, Fulham Road, London SW3 6JB, UK

author email corresponding author email

Genome Biology 2002, 3:reviews3009.1-3009.10doi:10.1186/gb-2002-3-7-reviews3009

Published:	26 June 2002

Subject areas: Cell biology, Genetics, Biochemistry and structural biology

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.