DUSPs, to MAP kinases and beyond
Open accessAbstract
Phosphatases are important regulators of intracellular signaling events, and their functions have been implicated in many biological processes. Dual-specificity phosphatases (DUSPs), whose family currently contains 25 members, are phosphatases that can dephosphorylate both tyrosine and serine/threonine residues of their substrates. The archetypical DUSP, DUSP1/MKP1, was initially discovered to regulate the activities of MAP kinases by dephosphorylating the TXY motif in the kinase domain. However, although DUSPs were discovered more than a decade ago, only in the past few years have their various functions begun to be described. DUSPs can be categorized based on the presence or absence of a MAP kinase-interacting domain into typical DUSPs and atypical DUSPs, respectively. In this review, we discuss the current understanding of how the activities of typical DUSPs are regulated and how typical DUSPs can regulate the functions of their targets. We also summarize recent findings from several in vivo DUSP-deficient mouse models that studied the involvement of DUSPs during the development and functioning of T cells. Finally, we discuss briefly the potential roles of DUSPs in the regulation of non-MAP kinase targets, as well as in the modulation of tumorigenesis.
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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 [77]
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Hallin, J., Engstrom, L. D., Hargis, L., Calinisan, A., Aranda, R., Briere, D. M., Sudhakar, N., Bowcut, V., Baer, B. R., Ballard, J. A., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1167 · Cited by 1,304 · see citing works
Negative feedback regulation of the ERK1/2 MAPK pathway
Lake, D., Corrêa, S. A. L., & Müller, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2297-8 · Cited by 565 · see citing works
Molecular basis of MAP kinase regulation
Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302 · see citing works
“which a conserved catalytic cysteine residue (HCxxxxxR) functions as a nucleophile.(34,77,78) However, the DUSP active site is shallow(11,34)—more sim-”
Background(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2018.11.001 · Cited by 71 · see citing works
Patrício, P., Mateus-Pinheiro, A., Irmler, M., Alves, N. D., Machado-Santos, A. R., Morais, M., Correia, J. S., Korostynski, M., Piechota, M., Stoffel, R., et al. (2015) · Neuropsychopharmacology · doi:10.1038/npp.2014.176 · Cited by 57 · see citing works
DUSP4-mediated accelerated T-cell senescence in idiopathic CD4 lymphopenia
Bignon, A., Régent, A., Klipfel, L., Desnoyer, A., de la Grange, P., Martinez, V., Lortholary, O., Dalloul, A., Mouthon, L., & Balabanian, K. (2015) · Blood · doi:10.1182/blood-2014-08-598565 · Cited by 51 · see citing works
Kumar, G. S., Zettl, H., Page, R., & Peti, W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.499178 · Cited by 12 · see citing works
“Of the 25 humanDUSPs, 10 have aKIM-containingMKBD thatmediates their direct interaction with MAPKs (8, 9).”
Background
- Authors
- Huang, C.-Y., & Tan, T.-H.
- Affiliations
- National Health Research Institutes (TW)
- Corresponding author
- Huang, Ching-Yu
- Venue
- Cell & Bioscience
- Published
- 2012
- Volume
- 2
- Issue
- 1
- Pages
- 24
- ISSN
- 2045-3701 (ISSN-L)
- PMC
- PMC3406950
- OpenAlex
- W2095821804
- Cited by
- 260
- References
- 94
- Citations by year
- 2026: 12 · 2025: 19 · 2024: 18 · 2023: 22 · 2022: 21 · 2021: 21 · 2020: 17 · 2019: 33 · 2018: 16 · 2017: 19 · 2016: 18 · 2015: 14 · 2014: 18 · 2013: 11 · 2012: 1
- FWCI
- 5.66
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Cell & Bioscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Science Council
- National Health Research Institutes
- National Institutes of Health
- 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, T cell development, carcinogenesis, intracellular signaling
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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