ArticleBiochemistry2013
Atomic structure of dual-specificity phosphatase 26, a novel p53 phosphatase.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- DUSP family phosphatases in cell signaling, inflammation, and chronic diseases.Journal of biomedical science · 2026Review
- Structural analysis of dual specificity phosphatases, the only type of protein tyrosine phosphatases found in humans and across diverse microorganisms.Journal of microbiology (Seoul, Korea) · 2025Review
- Variable Assembly and Procapsid Binding of Bacteriophage P22 Terminase Subunits in Solution.Pathogens (Basel, Switzerland) · 2024Article
- MAPKs in the early steps of senescence implemEMTation.Frontiers in cell and developmental biology · 2023Article
- A Review of DUSP26: Structure, Regulation and Relevance in Human Disease.International journal of molecular sciences · 2021Review
- Male-biased aganglionic megacolon in the TashT mouse model of Hirschsprung disease involves upregulation of p53 protein activity and Ddx3y gene expression.PLoS genetics · 2020Article
- Recognition of an α-helical hairpin in P22 large terminase by a synthetic antibody fragment.Acta crystallographica. Section D, Structural biology · 2020Article
- Upregulation of DUSP14 Affects Proliferation, Invasion and Metastasis, Potentially via Epithelial-Mesenchymal Transition and Is Associated with Poor Prognosis in Pancreatic Cancer.Cancer management and research · 2020Article
- Molecular Architecture of the Inositol Phosphatase Siw14.Biochemistry · 2019Article
- Structural and biochemical characterization of Siw14: A protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates.The Journal of biological chemistry · 2018Article
- Critical Roles of Dual-Specificity Phosphatases in Neuronal Proteostasis and Neurological Diseases.International journal of molecular sciences · 2017Review
- Structural and biochemical analysis of atypically low dephosphorylating activity of human dual-specificity phosphatase 28.PloS one · 2017Article
- Structural Insight into the Critical Role of the N-Terminal Region in the Catalytic Activity of Dual-Specificity Phosphatase 26.PloS one · 2016Article
- Structural Plasticity of the Protein Plug That Traps Newly Packaged Genomes in Podoviridae Virions.The Journal of biological chemistry · 2016Article
- Architecture of the Complex Formed by Large and Small Terminase Subunits from Bacteriophage P22.Journal of molecular biology · 2015Article
- Dimeric quaternary structure of human laforin.The Journal of biological chemistry · 2015Article
- Structure of human PIR1, an atypical dual-specificity phosphatase.Biochemistry · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Regulation of p53 phosphorylation is critical to control its stability and biological activity. Dual-specificity phosphatase 26 (DUSP26) is a brain phosphatase highly overexpressed in neuroblastoma, which has been implicated in dephosphorylating phospho-Ser20 and phospho-Ser37 in the p53 transactivation domain. In this paper, we report the 1.68 Å crystal structure of a catalytically inactive mutant (Cys152Ser) of DUSP26 lacking the first 60 N-terminal residues (ΔN60-C/S-DUSP26). This structure reveals the architecture of a dual-specificity phosphatase domain related in structure to Vaccinia virus VH1. DUSP26 adopts a closed conformation of the protein tyrosine phosphatase (PTP)-binding loop, which results in an unusually shallow active site pocket and buried catalytic cysteine. A water molecule trapped inside the PTP-binding loop makes close contacts both with main chain and with side chain atoms. The hydrodynamic radius (R(H)) of ΔN60-C/S-DUSP26 measured from velocity sedimentation analysis (R(H) ∼ 22.7 Å) and gel filtration chromatography (R(H) ∼ 21.0 Å) is consistent with an ∼18 kDa globular monomeric protein. Instead in crystal, ΔN60-C/S-DUSP26 is more elongated (R(H) ∼ 37.9 Å), likely because of the extended conformation of C-terminal helix α9, which swings away from the phosphatase core to generate a highly basic surface. As in the case of phosphatase MKP-4, we propose that a substrate-induced conformational change, possibly involving rearrangement of helix α9 with respect to the phosphatase core, allows DUSP26 to adopt a catalytically active conformation. The structural characterization of DUSP26 presented in this paper provides the first atomic insight into this disease-associated phosphatase.
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