DUSPs (dual-specificity phosphatases) are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues within the one substrate. DUSPs have been implicated as major modulators of critical signalling pathways that are dysregulated in various diseases. DUSPs can be divided into six subgroups on the basis of sequence similarity that include slingshots, PRLs (phosphatases of regenerating liver), Cdc14 phosphatases (Cdc is cell division cycle), PTENs (phosphatase and tensin homologues deleted on chromosome 10), myotubularins, MKPs (mitogen-activated protein kinase phosphatases) and atypical DUSPs. Of these subgroups, a great deal of research has focused on the characterization of the MKPs. As their name suggests, MKPs dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (extracellular-signal-regulated kinase), JNK (c-Jun N-terminal kinase) and p38 with specificity distinct from that of individual MKP proteins. Atypical DUSPs are mostly of low-molecular-mass and lack the N-terminal CH2 (Cdc25 homology 2) domain common to MKPs. The discovery of most atypical DUSPs has occurred in the last 6 years, which has initiated a large amount of interest in their role and regulation. In the past, atypical DUSPs have generally been grouped together with the MKPs and characterized for their role in MAPK signalling cascades. Indeed, some have been shown to dephosphorylate MAPKs. The current literature hints at the potential of the atypical DUSPs as important signalling regulators, but is crowded with conflicting reports. The present review provides an overview of the DUSP family before focusing on atypical DUSPs, emerging as a group of proteins with vastly diverse substrate specificity and function.
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Review Article|
February 25 2009
Dual-specificity phosphatases: critical regulators with diverse cellular targets
Kate I. Patterson;
Kate I. Patterson
1
*Cancer Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst 2010, Sydney, NSW, Australia
1To whom correspondence should be addressed (email k.patterson@garvan.org.au).
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Tilman Brummer;
Tilman Brummer
†Centre for Biological Systems Analysis (ZBSA) and Centre for Biological Signalling Studies (BIOSS), Faculty of Biology, Albert-Ludwigs University of Freiburg, 79104 Freiburg, Germany
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Philippa M. O'brien;
Philippa M. O'brien
*Cancer Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst 2010, Sydney, NSW, Australia
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Roger J. Daly
Roger J. Daly
*Cancer Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst 2010, Sydney, NSW, Australia
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Publisher: Portland Press Ltd
Received:
November 17 2008
Revision Received:
December 03 2008
Accepted:
December 04 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 418 (3): 475–489.
Article history
Received:
November 17 2008
Revision Received:
December 03 2008
Accepted:
December 04 2008
Citation
Kate I. Patterson, Tilman Brummer, Philippa M. O'brien, Roger J. Daly; Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem J 15 March 2009; 418 (3): 475–489. doi: https://doi.org/10.1042/BJ20082234
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