Dual-specificity phosphatases: critical regulators with diverse cellular targets

Patterson, Kate I.; Brummer, Tilman; O'brien, Philippa M.; Daly, Roger J.

doi:10.1042/bj20082234

Cited by 744Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

Dual-specificity phosphatases: critical regulators with diverse cellular targets

Patterson, Kate I., Brummer, Tilman, O'brien, Philippa M., Daly, Roger J.·2009·Biochemical Journal

DOI 10.1042/bj20082234

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Abstract

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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DUSPs/MKPs have two structured domains: an N-terminal MAPK binding domain (MKBD) and a C-terminal dual specificity phosphatase domain.
“However, unlike the KIM-PTPs, the DUSPs/MKPs have two structured domains: an N-terminal MAPK binding domain (MKBD) and a C-terminal dual specificity phosphatase domain [Fig.1(B), right].”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [34]
DUSPs dephosphorylate both serine/threonine and tyrosine residues using an enzymatic mechanism conserved with that of tyrosine phosphatases, in which a conserved catalytic cysteine residue (HCxxxxxR) functions as a nucleophile.
“DUSPs dephosphorylate both serine/threonine and tyrosine residues using an enzymatic mechanism conserved with that of tyrosine phosphatases in which a conserved catalytic cysteine residue (HCxxxxxR) functions as a nucleophile”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [34]
The DUSP active site is shallow, more similar to the depth of the active sites of serine/threonine specific phosphatases than to that of tyrosine phosphatases.
“the DUSP active site is shallow 11,34 -more similar to the depth of the active sites of serine/ threonine specific phosphatases [79][80][81] -when directly compared with that of tyrosine phosphatases, 38”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [34]
Ten DUSPs contain a MAPK binding domain (MKBD) with a KIM interaction sequence that is required for a direct interaction with MAPKs.
“Ten DUSPs contain a MAPK binding domain (MKBD) with a KIM interaction sequence that is required for a direct interaction with MAPKs.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [34]

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Authors: Patterson, K. I., Brummer, T., O'brien, P. M., & Daly, R. J.
Affiliations: Garvan Institute of Medical Research (AU)
University of Freiburg (DE)
Cancer Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst 2010, Sydney, NSW, Australia
ORCID: Patterson, Kate I.
Brummer, Tilman
Daly, Roger J.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2009-02-25
Volume: 418
Issue: 3
Pages: 475-489
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20082234
OpenAlex: W2324138891
Cited by: 744
References: 189
Citations by year: 2026: 25 · 2025: 22 · 2024: 39 · 2023: 30 · 2022: 41 · 2021: 48 · 2020: 32 · 2019: 39 · 2018: 35 · 2017: 58 · 2016: 50 · 2015: 45 · 2014: 45 · 2013: 60 · 2012: 60
FWCI: 4.32
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: dual-specificity phosphatase, mitogen-activated protein kinase phosphatase, MAPK signaling, ERK, JNK, p38 MAPK, dephosphorylation, protein phosphatase, Cdc14 phosphatase, myotubularin, slingshot
MeSH terms: Animals, Humans, Membrane Proteins, Phosphoric Monoester Hydrolases, Phosphoprotein Phosphatases, Protein Tyrosine Phosphatases, Cell Cycle Proteins, Cyclin-Dependent Kinase Inhibitor Proteins, PTEN Phosphohydrolase, Protein Tyrosine Phosphatases, Non-Receptor, Dual-Specificity Phosphatases, Dual Specificity Phosphatase 1, Mitogen-Activated Protein Kinase Phosphatases, Dual Specificity Phosphatase 3

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Dual-specificity phosphatases: critical regulators with diverse cellular targets

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