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August 5, 2024Frontiers in Chemical BiologyOpen Access

Structural and kinetic characterization of DUSP5 with a Di-phosphorylated tripeptide substrate from the ERK activation loop

Andrea Imhoff Noreena L. Sweeney Robert D. Bongard Raulia Syrlybaeva Ankan Gupta Edgar Del Carpio Marat R. Talipov Costanza Garcia-Keller Debbie C. Crans Ramani Ramchandran Daniel S. Sem

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Abstract

Dual specific phosphatases (DUSPs) are mitogen-activated protein kinase (MAPK) regulators, which also serve as drug targets for treating various vascular diseases. Previously, we have presented mechanistic characterizations of DUSP5 and its interaction with pERK, proposing a dual active site.

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Imhoff et al. (2024) studied this question.

synapsesocial.com/papers/68e5d588b6db64358756bd9d https://doi.org/10.3389/fchbi.2024.1385560

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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Protein expression, characterization and activity comparisons of wild type and mutant DUSP5 proteinsOriginal Research · 2014 · 13 citations
2DUSP5-mediated inhibition of smooth muscle cell proliferation suppresses pulmonary hypertension and right ventricular hypertrophyCase-Control Study · 2021 · 16 citations
3Dual-Specificity Protein Phosphatases Targeting Extracellular Signal-Regulated Kinases: Friends or Foes in the Biology of Cancer?2025 · 12 citations
4DUSP5 suppresses esophageal squamous cell carcinoma by counteracting macrophage-derived AREG-ERK1/2 signaling and disrupting an oncogenic ERK1/2-ELK1-DUSP5 feedback circuitryOriginal Research · 2026
5The dual specificity phosphatase 2 act as distal regulatory node in T cell signalingOriginal Research · 2026

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