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Curr Opin Cell Biol. 2000 Apr;12(2):186-92.

Protein phosphatases and the regulation of mitogen-activated protein kinase signalling.

Author information

1
Molecular Pharmacology Unit, Imperial Cancer Research Fund, Biomedical Research Centre, Level 5, Ninewells Hospital, Dundee, DD1 9SY, UK. S.Keyse@icrf.icnet.uk

Abstract

The magnitude and duration of signalling through mitogen- and stress-activated kinases are critical determinants of biological effect. This reflects a balance between the activities of upstream activators and a complex regulatory network of protein phosphatases. These mitogen-activated protein kinase phosphatases include both dual-specificity (threonine/tyrosine) and tyrosine-specific enzymes, and recent evidence suggests that a single mitogen-activated protein kinase isoform may be acted upon by both classes of protein phosphatase. In both cases, substrate selectivity is determined by specific protein-protein interactions mediated through noncatalytic amino-terminal mitogen-activated protein kinase binding domains. Future challenges include the determination of exactly how this network of protein phosphatases interacts selectively with mitogen-activated protein kinase signalling complexes to achieve precise regulation of these key pathways in mammalian cells.

PMID:
10712927
[Indexed for MEDLINE]

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