ArticleFrontiers in chemical biology2024
Structural and kinetic characterization of DUSP5 with a Di-phosphorylated tripeptide substrate from the ERK activation loop.
Article in Frontiers in chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- ERK autoinhibition mechanism informs a drug combination strategy.Protein science : a publication of the Protein Society · 2026Article
- Applications of Carbon Dots and Graphene Quantum Dots in Treatment of Diabetes.Molecules (Basel, Switzerland) · 2026Review
- Article
- Design and synthesis of 3,4-seco-lupane triterpene-tryptamine derivatives and revealing their anti-bladder cancer mechanisms by combining TCGA and transcriptomic approaches.Scientific reports · 2025Article
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Abstract
Introduction: 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. Methods: Herein, we characterize the interactions between the DUSP5 phosphatase domain and the pT-E-pY activation loop of ERK2, with specific active site assignments. We also report the full NMR chemical shift assignments of DUSP5 that now enable chemical shift perturbation and dynamics studies. Results and Discussion: Both phosphates of the pT-E-pY tripeptide are dephosphorylated, based on Summary: These studies indicate a preference for pY before pT binding, but with ability to bind and dephosphorylate both residues, and with a dynamic active site pocket that accommodates multiple tripeptide orientations.
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