Anton Bennett, PhD
Dorys McConnell Duberg Professor of Pharmacology and Professor of Comparative MedicineCards
Additional Titles
Director, Yale Center for Molecular and Systems Metabolism (YMSM)
Director of Diversity and Inclusion, Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Contact Info
Pharmacology
PO Box 208066, 333 Cedar Street
New Haven, CT 06520-8066
United States
Appointments
Additional Titles
Director, Yale Center for Molecular and Systems Metabolism (YMSM)
Director of Diversity and Inclusion, Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Contact Info
Pharmacology
PO Box 208066, 333 Cedar Street
New Haven, CT 06520-8066
United States
Appointments
Additional Titles
Director, Yale Center for Molecular and Systems Metabolism (YMSM)
Director of Diversity and Inclusion, Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Contact Info
Pharmacology
PO Box 208066, 333 Cedar Street
New Haven, CT 06520-8066
United States
About
Titles
Dorys McConnell Duberg Professor of Pharmacology and Professor of Comparative Medicine
Director, Yale Center for Molecular and Systems Metabolism (YMSM); Director of Diversity and Inclusion, Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Appointments
Pharmacology
ProfessorPrimaryComparative Medicine
ProfessorSecondary
Other Departments & Organizations
- Bennett Lab
- Cancer Signaling Networks
- Comparative Medicine
- Diabetes Research Center
- Liver Center
- Molecular Medicine, Pharmacology, and Physiology
- MORE
- Neuroscience Track
- Pharmacology
- Primary Faculty
- Program in Translational Biomedicine (PTB)
- Vascular Biology and Therapeutics Program
- Yale Cancer Center
- Yale Center for Molecular and Systems Metabolism (YMSM)
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
- Yale Stem Cell Center
- Yale Ventures
Education & Training
- Postdoc
- Cold Spring Harbor Laboratories (1998)
- Postdoc
- Harvard Medical School (1995)
- PhD
- New York Medical College (1993)
Research
Overview
Cell proliferation, cell differentiation and death are controlled by signaling pathways that are mediated by protein tyrosyl phosphorylation. The net cellular level of protein tyrosyl phosphorylation is regulated by the intrinsic and opposing activities of protein tyrosine kinases and protein tyrosine phosphatases (PTPs). Dysregulation of the net level of tyrosyl phosphorylation causes cancer, diabetes, cardiovascular disease and developmental abnormalities.
We focus our studies on how PTPs regulate cell signaling by controlling protein tyrosyl dephosphorylation. We are also exploring how PTPs participate in the pathogenesis of diseases such as obesity and diabetes, cardiovascular disease and developmental abnormalities. These research efforts are being accomplished by using integrated approaches that encompass cell biology, genetics, protein biochemistry, cell imaging and animal models. Our long-term research goals are to uncover the function of PTPs in order to identify whether these enzymes might serve as novel therapeutic targets for the treatment of human diseases.
For further information please visit the Bennett Lab website - Home | Bennett Lab (bennett-lab.org)
Medical Research Interests
ORCID
0000-0001-5187-7599- View Lab Website
Bennett Lab
Research at a Glance
Yale Co-Authors
Publications Timeline
Research Interests
Naftali Kaminski, MD
Sravan Perla, PhD, MSc
Xiaoyong Yang, PhD
Farida Ahangari, MD
Argyrios Tzouvelekis, MD, PhD
Carlos Fernandez-Hernando, PhD
Signal Transduction
Publications
2024
Mitogen-Activated Protein Kinase Phosphatase-5 is Required for TGF-β Signaling Through a JNK-Dependent Pathway
Dorry S, Perla S, Bennett A. Mitogen-Activated Protein Kinase Phosphatase-5 is Required for TGF-β Signaling Through a JNK-Dependent Pathway. Molecular And Cellular Biology 2024, ahead-of-print: 1-15. PMID: 39607740, DOI: 10.1080/10985549.2024.2426665.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseTGF-b signalingMKP-5JNK-dependent pathwayFamily of protein phosphatasesNon-canonical sitesJNK-dependent mannerP38 mitogen-activated protein kinaseMitogen-activated protein kinase phosphatase-5JNK-dependentTranscriptional activityProtein phosphatasesTranscriptome analysisRNA sequencingProtein kinaseJNK inactivationNuclear translocationSignaling activityTGF-bSmad2 phosphorylationPharmacological inhibitionDrivers of fibrosisTissue fibrosisFactor BPathwaySpatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT
Ong Q, Lim L, Goh C, Liao Y, Chan S, Lim C, Kam V, Yap J, Tseng T, Desrouleaux R, Wang L, Ler S, Lim S, Kim S, Sobota R, Bennett A, Han W, Yang X. Spatiotemporal control of subcellular O-GlcNAc signaling using Opto-OGT. Nature Chemical Biology 2024, 1-9. PMID: 39543398, DOI: 10.1038/s41589-024-01770-7.Peer-Reviewed Original ResearchConceptsO-GlcNAc transferaseO-GlcNAcLocalized to specific subcellular sitesResponse to insulin stimulationPost-translational modification of intracellular proteinsModification of intracellular proteinsO-GlcNAc signalingPost-translational modificationsTargeting O-GlcNAc transferaseSpatiotemporal controlMulticellular organismsOGT activityOrganelle functionO-GlcNAcylationSubcellular sitesMTORC activitySignal transductionIntracellular proteinsNutrient-sensing signalsCell signalingInsulin stimulationPlasma membraneGene expressionRegulatory mechanismsAkt phosphorylationmiR-33 deletion in hepatocytes attenuates NAFLD-NASH-HCC progression
Fernández-Tussy P, Cardelo M, Zhang H, Sun J, Price N, Boutagy N, Goedeke L, Cadena-Sandoval M, Xirouchaki C, Brown W, Yang X, Pastor-Rojo O, Haeusler R, Bennett A, Tiganis T, Suárez Y, Fernández-Hernando C. miR-33 deletion in hepatocytes attenuates NAFLD-NASH-HCC progression. JCI Insight 2024, 9: e168476. PMID: 39190492, PMCID: PMC11466198, DOI: 10.1172/jci.insight.168476.Peer-Reviewed Original ResearchConceptsMiR-33Regulation of biological processesMitochondrial fatty acid oxidationRegulation of lipid metabolismNon-alcoholic fatty liver diseaseDevelopment of effective therapeuticsFatty acid oxidationLipid synthesisProgression of non-alcoholic fatty liver diseaseMitochondrial functionTarget genesBiological processesComplex diseasesNon-alcoholic steatohepatitisLipid accumulationDeletionDevelopment of non-alcoholic fatty liver diseasePathway activationLipid metabolismProgress to non-alcoholic steatohepatitisAcid oxidationHCC progressionEffective therapeuticsTherapeutic targetHepatocellular carcinomaMAP kinase phosphatase-1 inhibition of p38α within lung myofibroblasts is essential for spontaneous fibrosis resolution
Fortier S, Walker N, Penke L, Baas J, Shen Q, Speth J, Huang S, Zemans R, Bennett A, Peters-Golden M. MAP kinase phosphatase-1 inhibition of p38α within lung myofibroblasts is essential for spontaneous fibrosis resolution. Journal Of Clinical Investigation 2024, 134: e172826. PMID: 38512415, PMCID: PMC11093610, DOI: 10.1172/jci172826.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsMAPK phosphatase 1Fibrosis resolutionPulmonary fibrosisSpontaneous resolutionLung fibrosisBleomycin-induced lung fibrosisLung fibroblastsProgressive pulmonary fibrosisFibroblast-specific deletionExperimental lung fibrosisCells to apoptosisLung injuryRegulation of MAPK activityApoptosis-resistant myofibroblastsTransgenic miceResident fibroblastsTissue injuryFibrosisLung myofibroblastsLoss-of-function studiesGain- and loss-of-function studiesLungVX-702MyofibroblastsMAPK activationSkeletal muscle TET3 promotes insulin resistance through destabilisation of PGC-1α
Liu B, Xie D, Huang X, Jin S, Dai Y, Sun X, Li D, Bennett A, Diano S, Huang Y. Skeletal muscle TET3 promotes insulin resistance through destabilisation of PGC-1α. Diabetologia 2024, 67: 724-737. PMID: 38216792, PMCID: PMC10904493, DOI: 10.1007/s00125-023-06073-5.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsTen-eleven translocationMuscle insulin sensitivityRNA-seqPGC-1aRegulation of muscle insulin sensitivityType 2 diabetesAnalysis of RNA-seqResponse to environmental cuesGenome-wide expression profilingWild-typeHFD-fedHFD-induced insulin resistanceHigh-fat diet (HFD)-inducedExpression levelsMaintenance of glucoseSkeletal muscle insulin sensitivityAccession numbersSkeletal muscleEnhanced glucose toleranceFamily dioxygenasesMitochondrial respirationSkeletal muscle of humansEnvironmental cuesMitochondrial functionBiological processes
2023
Identification of Protein Tyrosine Phosphatase (PTP) Substrates
Perla S, Qiu B, Dorry S, Yi J, Bennett A. Identification of Protein Tyrosine Phosphatase (PTP) Substrates. Methods In Molecular Biology 2023, 2743: 123-133. PMID: 38147212, PMCID: PMC11610242, DOI: 10.1007/978-1-0716-3569-8_8.Peer-Reviewed Original ResearchMKP1 promotes nonalcoholic steatohepatitis by suppressing AMPK activity through LKB1 nuclear retention
Qiu B, Lawan A, Xirouchaki C, Yi J, Robert M, Zhang L, Brown W, Fernández-Hernando C, Yang X, Tiganis T, Bennett A. MKP1 promotes nonalcoholic steatohepatitis by suppressing AMPK activity through LKB1 nuclear retention. Nature Communications 2023, 14: 5405. PMID: 37669951, PMCID: PMC10480499, DOI: 10.1038/s41467-023-41145-5.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsTeaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery
Bennett A. Teaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery. Journal Of Biological Chemistry 2023, 299: 104731. PMID: 37080392, PMCID: PMC10193000, DOI: 10.1016/j.jbc.2023.104731.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsIdentification of substratesSubstrate discoveryProtein tyrosineProtein substratesInteraction networksBreast cancer cell modelsCancer cell modelsFunctional interactionNovel targetVersatile new toolNew toolCell modelComplete understandingRecent studiesOld dog new tricksNew tricksInteractorsPTP1B.PTP1BPTPMutationsSubstrateEnzymeTyrosinePathwaySH2 Domain-Containing Phosphatase-SHP2 Attenuates Fibrotic Responses through Negative Regulation of Mitochondrial Metabolism in Lung Fibroblasts
Karampitsakos T, Galaris A, Barbayianni I, DeIuliis G, Ahangari F, Sampsonas F, Sotiropoulou V, Aidinis V, Bennett A, Herazo-Maya J, Xylourgidis N, Bakakos P, Bouros D, Kaminski N, Tzouvelekis A. SH2 Domain-Containing Phosphatase-SHP2 Attenuates Fibrotic Responses through Negative Regulation of Mitochondrial Metabolism in Lung Fibroblasts. Diagnostics 2023, 13: 1166. PMID: 36980473, PMCID: PMC10047203, DOI: 10.3390/diagnostics13061166.Peer-Reviewed Original ResearchMitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable?
Shillingford S, Bennett A. Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable? The Annual Review Of Pharmacology And Toxicology 2023, 63: 617-636. PMID: 36662585, PMCID: PMC10127142, DOI: 10.1146/annurev-pharmtox-051921-121923.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsMitogen-activated protein kinaseSmall molecule inhibitionProtein kinaseCritical cellular functionsInhibition of PTPsProtein tyrosineCellular functionsProtein substratesPhosphorylated proteinsCell signalingTyrosine residuesAttractive therapeutic targetCellular effectsKinaseNumerous diseasesPTPDiscovery toolTherapeutic developmentTherapeutic targetMetabolic diseasesInhibitionDephosphorylationSignalingMKPProtein
Academic Achievements & Community Involvement
honor Blavatnik Innovation Award
Yale School of Medicine AwardBlavatnik FundDetails06/01/2017United Stateshonor Burroughs-Wellcome Award for New Investigators in Pharmacology
UnknownDetails01/01/2001United Stateshonor Pharmaceuticals Manufacturers Association Young Investigators Award
UnknownDetails01/01/2000United States
News
News
- January 02, 2024
Building Community to Advance Metabolic Science
- December 13, 2023
YBDIC: Transforming the Landscape of Inclusivity in Biological and Biomedical Sciences at Yale School of Medicine
- May 24, 2023Source: Yale Ventures
Blavatnik Fund for Innovation at Yale Awards $2.5 Million to 11 Faculty-Led Projects
- December 12, 2022Source: Yale Ventures
Eight Yale Faculty Take Home Awards at the 2022 Yale Life Sciences Pitchfest
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Pharmacology
PO Box 208066, 333 Cedar Street
New Haven, CT 06520-8066
United States
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