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An allosteric site on MKP5 reveals a strategy for small-molecule inhibition

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Optimizing Expression and Solubility of Proteins in E. coli Using Modified Media and Induction Parameters
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Structure and regulation of MAPK phosphatases
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Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase
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Leveraging Reciprocity to Identify and Characterize Unknown Allosteric Sites in Protein Tyrosine Phosphatases
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Transforming Growth Factor-β1 Induces the Differentiation of Myogenic Cells into Fibrotic Cells in Injured Skeletal Muscle
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Mechanisms of TGF-β Signaling from Cell Membrane to the Nucleus
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Drugging the Undruggable: Therapeutic Potential of Targeting Protein Tyrosine Phosphatases
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Structural and Dynamic Insights into the Mechanism of Allosteric Signal Transmission in ERK2-Mediated MKP3 Activation
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Convergent Synthesis of Diverse Nitrogen Heterocycles via Rh(III)-Catalyzed C–H Conjugate Addition/Cyclization Reactions
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Structural Basis for the Recognition of a Bisphosphorylated MAP Kinase Peptide by Human VHR Protein Phosphatase
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Allosteric Competitive Inhibitors of the Glucose-1-phosphate Thymidylyltransferase (RmlA) from Pseudomonas aeruginosa
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LigPlot+: Multiple Ligand–Protein Interaction Diagrams for Drug Discovery
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A non‐redundant role for MKP5 in limiting ROS production and preventing LPS‐induced vascular injury
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Regulation of innate and adaptive immune responses by MAP kinase phosphatase 5
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ATP-competitive inhibitors of the mitotic kinesin KSP that function via an allosteric mechanism
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A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation
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DUSP10 regulates intestinal epithelial cell growth and colorectal tumorigenesis
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Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, MKP-5
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Enzymatic Activity and Substrate Specificity of Mitogen-activated Protein Kinase p38α in Different Phosphorylation States
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Synthesis of New 3-Methylthio-4, 5, 6, 7-tetrahydro Benzo[c]thiophene-4-ones
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Pharmacological therapeutics targeting the secondary defects and downstream pathology of Duchenne muscular dystrophy
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Geneious Basic: An integrated and extendable desktop software platform for the organization and analysis of sequence data
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CAVER Analyst 1.0: graphic tool for interactive visualization and analysis of tunnels and channels in protein structures
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UniProt: the Universal Protein knowledgebase
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UniProt: the universal protein knowledgebase
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MAP kinase phosphatase‐1 deficiency impairs skeletal muscle regeneration and exacerbates muscular dystrophy
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Targeting Fibrosis in Duchenne Muscular Dystrophy
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Cell Signaling and Stress Responses
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PHENIX: a comprehensive Python-based system for macromolecular structure solution
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Phaser crystallographic software
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MolProbity : all-atom structure validation for macromolecular crystallography
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XDS
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PHENIX : a comprehensive Python-based system for macromolecular structure solution
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Features and development of Coot
inferredcites →https://doi.org/10.1110/ps.062712807openalex-snapshot
Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5
inferredcites →https://doi.org/10.1111/j.1742-4658.2012.08716.xopenalex-snapshot
Dual‐specificity MAP kinase phosphatases (MKPs)
inferredcites →https://doi.org/10.1111/jnc.12463openalex-snapshot
Molecular mechanism of ERK dephosphorylation by striatal‐enriched protein tyrosine phosphatase
inferredcites →https://doi.org/10.1126/science.280.5367.1262openalex-snapshot
Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase
inferredcites →https://doi.org/10.1126/science.7540771openalex-snapshot
Structural Basis for Phosphotyrosine Peptide Recognition by Protein Tyrosine Phosphatase 1B
inferredcites →https://doi.org/10.1126/scisignal.2002241openalex-snapshot
A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5
inferredcites →https://doi.org/10.1128/mmbr.00031-10openalex-snapshot
Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases
inferredcites →https://doi.org/10.1152/ajpcell.00173.2013openalex-snapshot
Cellular Mechanisms of Tissue Fibrosis. 4. Structural and functional consequences of skeletal muscle fibrosis
inferredcites →https://doi.org/10.1152/ajplung.00264.2018openalex-snapshot
Role of dual-specificity protein phosphatase DUSP10/MKP-5 in pulmonary fibrosis
inferredcites →https://doi.org/10.1161/circulationaha.106.679589openalex-snapshot
Mitogen-Activated Protein Kinases in Heart Development and Diseases
inferredcites →https://doi.org/10.1172/jci64375openalex-snapshot
Improved regenerative myogenesis and muscular dystrophy in mice lacking Mkp5
inferredcites →https://doi.org/10.1371/journal.pone.0072340openalex-snapshot
Dual-Specificity Phosphatase 10 Controls Brown Adipocyte Differentiation by Modulating the Phosphorylation of P38 Mitogen-Activated Protein Kinase
inferredcites →https://doi.org/10.2147/ndt.s93873openalex-snapshot
Current and emerging treatment strategies for Duchenne muscular dystrophy
inferredcites →https://doi.org/10.2337/db17-0826openalex-snapshot
Skeletal Muscle–Specific Deletion of MKP-1 Reveals a p38 MAPK/JNK/Akt Signaling Node That Regulates Obesity-Induced Insulin Resistance
inferredcites →https://doi.org/10.4049/jimmunol.1301863openalex-snapshot
MAPK Phosphotase 5 Deficiency Contributes to Protection against Blood-Stage Plasmodium yoelii 17XL Infection in Mice

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.47191/ijpbms/v1-i7-02openalex-extracted
The Protein Tyrosine Phosphatase PTB1B Role in the Development of Obesity, Diabetes, and Cancer and its Potential Inhibitors
inferred← citeshttps://doi.org/10.1016/j.cellsig.2021.110033openalex-snapshot
Dual specific phosphatases (DUSPs) in cardiac hypertrophy and failure
inferred← citeshttps://doi.org/10.1016/j.ejmech.2022.114712openalex-snapshot
Defining the structure-activity relationship for a novel class of allosteric MKP5 inhibitors
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102617openalex-snapshot
A novel site on dual-specificity phosphatase MKP7/DUSP16 is required for catalysis and MAPK binding
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.110570openalex-snapshot
BCI inhibits MKP3 by targeting the kinase-binding domain and disrupting ERK2 interaction
inferred← citeshttps://doi.org/10.1016/j.tem.2025.05.002openalex-snapshot
MAP kinase phosphatases in metabolic diseases
inferred← citeshttps://doi.org/10.1021/acs.jcim.1c01267openalex-snapshot
Uncovering the Dominant Motion Modes of Allosteric Regulation Improves Allosteric Site Prediction
inferred← citeshttps://doi.org/10.1038/s41467-023-41145-5openalex-snapshot
MKP1 promotes nonalcoholic steatohepatitis by suppressing AMPK activity through LKB1 nuclear retention
inferred← citeshttps://doi.org/10.1038/s41467-025-62150-wopenalex-snapshot
Dynamic and structural insights into allosteric regulation on MKP5 a dual-specificity phosphatase
inferred← citeshttps://doi.org/10.1038/s41573-022-00618-wopenalex-snapshot
Targeting protein phosphatases in cancer immunotherapy and autoimmune disorders
inferred← citeshttps://doi.org/10.1042/bst20201308openalex-snapshot
Functional interrogation and therapeutic targeting of protein tyrosine phosphatases
inferred← citeshttps://doi.org/10.1042/etls20200258openalex-snapshot
Evolution of biophysical tools for quantitative protein interactions and drug discovery
inferred← citeshttps://doi.org/10.1080/10985549.2024.2426665openalex-snapshot
Mitogen-Activated Protein Kinase Phosphatase-5 is Required for TGF-β Signaling Through a JNK-Dependent Pathway
inferred← citeshttps://doi.org/10.1101/2024.06.27.600976openalex-snapshot
MAPK Phosphatase-5 is required for TGF-β signaling through a JNK-dependent pathway
inferred← citeshttps://doi.org/10.1146/annurev-pharmtox-051921-121923openalex-snapshot
Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable?
inferred← citeshttps://doi.org/10.1146/annurev-physiol-022724-105540openalex-snapshot
Protein Tyrosine Phosphatases in Metabolism: A New Frontier for Therapeutics
inferred← citeshttps://doi.org/10.2533/chimia.2022.460openalex-snapshot
Protein Phosphatases: A Neglected Target Family for Drug Discovery
inferred← citeshttps://doi.org/10.33696/signaling.1.025openalex-snapshot
Improving Obesity and Insulin Resistance by Targeting Skeletal Muscle MKP-1
inferred← citeshttps://doi.org/10.3390/ijms21207515openalex-snapshot
Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases
inferred← citeshttps://doi.org/10.71150/jm.2506006openalex-snapshot
Structural analysis of dual specificity phosphatases, the only type of protein tyrosine phosphatases found in humans and across diverse microorganisms
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