2025
FAK inhibition combined with the RAF-MEK clamp avutometinib overcomes resistance to targeted and immune therapies in BRAF V600E melanoma
Lubrano S, Cervantes-Villagrana R, Faraji F, Ramirez S, Sato K, Adame-Garcia S, Officer A, Arang N, Rigiracciolo D, Anguiano Quiroz P, Martini C, Wang Y, Ferguson F, Bacchiocchi A, Halaban R, Coma S, Holmen S, Pachter J, Aplin A, Gutkind J. FAK inhibition combined with the RAF-MEK clamp avutometinib overcomes resistance to targeted and immune therapies in BRAF V600E melanoma. Cancer Cell 2025, 43: 428-445.e6. PMID: 40020669, PMCID: PMC11903146, DOI: 10.1016/j.ccell.2025.02.001.Peer-Reviewed Original ResearchConceptsBRAF V600E melanomaFocal adhesion kinaseV600E melanomaFAK inhibitorActivated focal adhesion kinaseFocal adhesion kinase inhibitionRaf-MEKActivation of focal adhesion signalingFocal adhesion kinase inhibitorResistance to BRAFiSyngeneic mouse modelMAPK pathway inhibitionFocal adhesion signalingPro-apoptotic activityMelanoma patientsAdhesion signalingImmune therapyBRAF mutationsBRAFiTranscriptome analysisMelanomaMouse modelPathway inhibitionBRAFMelanoma cells
2024
Ezrin drives adaptation of monocytes to the inflamed lung microenvironment
Gudneppanavar R, Di Pietro C, H Öz H, Zhang P, Cheng E, Huang P, Tebaldi T, Biancon G, Halene S, Hoppe A, Kim C, Gonzalez A, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. Cell Death & Disease 2024, 15: 864. PMID: 39613751, PMCID: PMC11607083, DOI: 10.1038/s41419-024-07255-8.Peer-Reviewed Original ResearchConceptsActivation of focal adhesion kinaseExtracellular matrixActin-binding proteinsFocal adhesion kinaseLung extracellular matrixKnock-out mouse modelProtein kinase signalingCortical cytoskeletonLoss of ezrinKinase signalingPlasma membraneCell migrationSignaling pathwayEzrinResponse to lipopolysaccharideTissue-resident macrophagesMouse modelLipopolysaccharideCytoskeletonEzrin expressionLung microenvironmentKinaseMonocyte recruitmentProteinAktPreclinical evaluation of avutometinib and defactinib in high‐grade endometrioid endometrial cancer
Hartwich T, Mansolf M, Demirkiran C, Greenman M, Bellone S, McNamara B, Nandi S, Alexandrov L, Yang‐Hartwich Y, Coma S, Pachter J, Santin A. Preclinical evaluation of avutometinib and defactinib in high‐grade endometrioid endometrial cancer. Cancer Medicine 2024, 13: e70210. PMID: 39240189, PMCID: PMC11378359, DOI: 10.1002/cam4.70210.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic Combined Chemotherapy ProtocolsBenzamidesCarcinoma, EndometrioidCell Line, TumorCell ProliferationEndometrial NeoplasmsExome SequencingFemaleFocal Adhesion Kinase 1HumansImidazolesMiceNeoplasm GradingOxazepinesProtein Kinase InhibitorsPyrazinesSulfonamidesXenograft Model Antitumor AssaysConceptsFocal adhesion kinaseWhole-exome sequencingEndometrial cancer cell linesVS-4718Cell linesRas/MAPK pathwayPhosphorylated focal adhesion kinaseWestern blot assayWhole-exome sequencing resultsRAF/MEK inhibitionEAC cell linesBlot assayP-FAKGenetic landscapeCell cycleEndometrial cancerGenetic derangementsDefactinibP-MEKGrowth inhibitionRAF/MEKRas/MAPKCell viabilityP-ERKHigh-grade endometrial cancerPreclinical in vitro and in vivo activity of the RAF/MEK clamp avutometinib in combination with FAK inhibition in uterine carcinosarcomas
Demirkiran C, Greenman M, Bellone S, McNamara B, Hartwich T, Manavella D, Mutlu L, Zipponi M, Yang-Hartwich Y, Yang K, Ratner E, Schwartz P, Coma S, Pachter J, Santin A. Preclinical in vitro and in vivo activity of the RAF/MEK clamp avutometinib in combination with FAK inhibition in uterine carcinosarcomas. Gynecologic Oncology 2024, 187: 12-20. PMID: 38703673, DOI: 10.1016/j.ygyno.2024.04.010.Peer-Reviewed Original ResearchFocal adhesion kinaseUC cell linesWhole-exome-sequencingFAK inhibitorCell linesFocal adhesion kinase inhibitionPhosphorylated (p)‑FAKWestern blot assayRAF/MEK inhibitionUterine carcinosarcomaRAS/MAPK pathway genesPreclinical in vitroBlot assayVS-4718Cell cycle assayGenetic landscapePathway genesMAP2KGenetic alterationsDecreased p-ERKCycle assaySuperior tumor growth inhibitionBiologically aggressive tumorsGrowth inhibitionIn vitro activity
2019
Pyk2 Signaling through Graf1 and RhoA GTPase Is Required for Amyloid-β Oligomer-Triggered Synapse Loss
Lee S, Salazar SV, Cox TO, Strittmatter SM. Pyk2 Signaling through Graf1 and RhoA GTPase Is Required for Amyloid-β Oligomer-Triggered Synapse Loss. Journal Of Neuroscience 2019, 39: 1910-1929. PMID: 30626696, PMCID: PMC6407289, DOI: 10.1523/jneurosci.2983-18.2018.Peer-Reviewed Original ResearchConceptsDendritic spine lossGenetic variationRhoA GTPaseSynapse lossSpine lossBiochemical basisGTPase-activating proteinsFocal adhesion kinasePyk2 functionPyk2 tyrosine kinasePostsynaptic sitesTyrosine kinase Pyk2Disease riskKinase-dependent mechanismOverexpression of Pyk2Dendritic spine densityAdhesion kinaseTransgenic mouse modelBiochemical isolationPyk2 kinaseAlzheimer's disease riskDendritic spine stabilityKinase Pyk2Late-onset Alzheimer's disease (LOAD) riskActin control
2017
The RNA-editing enzyme ADAR promotes lung adenocarcinoma migration and invasion by stabilizing FAK
Amin E, Liu Y, Deng S, Tan K, Chudgar N, Mayo M, Sanchez-Vega F, Adusumilli P, Schultz N, Jones D. The RNA-editing enzyme ADAR promotes lung adenocarcinoma migration and invasion by stabilizing FAK. Science Signaling 2017, 10 PMID: 28928239, PMCID: PMC5771642, DOI: 10.1126/scisignal.aah3941.Peer-Reviewed Original ResearchConceptsFocal adhesion kinaseRNA editing enzyme ADARPresence of ADARsAnalysis of gene expression patternsGenome-wide studiesLung adenocarcinoma cellsRNA-binding proteinsCell migration pathwaysGene expression patternsStabilized transcriptsIntron sitesADARProtein abundanceBinding proteinIncreased abundanceExpression patternsMolecular analysisStage I LUAD patientsPharmacological inhibitionProteinMesenchymal propertiesPotential therapeutic applicationsProtein levelsTranscriptionGenes
2016
Proteomic Profiling Identifies PTK2/FAK as a Driver of Radioresistance in HPV-negative Head and Neck Cancer
Skinner HD, Giri U, Yang L, Woo SH, Story MD, Pickering CR, Byers LA, Williams MD, El-Naggar A, Wang J, Diao L, Shen L, Fan YH, Molkentine DP, Beadle BM, Meyn RE, Myers JN, Heymach JV. Proteomic Profiling Identifies PTK2/FAK as a Driver of Radioresistance in HPV-negative Head and Neck Cancer. Clinical Cancer Research 2016, 22: 4643-4650. PMID: 27036135, PMCID: PMC5061056, DOI: 10.1158/1078-0432.ccr-15-2785.Peer-Reviewed Original ResearchConceptsHPV-negative HNSCC cell linesHPV-negative HNSCCHNSCC cell linesTargetable biomarkersHuman papillomavirusIndependent cohortCandidate biomarkersPoor disease-free survivalNeck squamous cell carcinomaBiomarker of radioresistanceDisease-free survivalSquamous cell carcinomaDisease-related mortalityMerit further evaluationCell linesFAK inhibitionG2-M arrestFocal adhesion kinaseAdvanced HNSCCWorse DFSCancer Genome AtlasCell carcinomaPharmacologic blockadeCancer subgroupsFAK overexpression
2012
FAK promotes recruitment of talin to nascent adhesions to control cell motility
Lawson C, Lim ST, Uryu S, Chen XL, Calderwood DA, Schlaepfer DD. FAK promotes recruitment of talin to nascent adhesions to control cell motility. Journal Of Cell Biology 2012, 196: 223-232. PMID: 22270917, PMCID: PMC3265949, DOI: 10.1083/jcb.201108078.Peer-Reviewed Original ResearchConceptsFocal adhesion kinaseNascent adhesionsCell motilityCell migrationRecruitment of talinCytoskeletal protein talinTension-independent mannerCytoskeletal-associated proteinDirect binding siteTalin associationProtein talinFAK recruitmentAdhesion dynamicsAdhesion kinaseFAK localizationTalinAdhesion sitesTalin cleavageIntegrin receptorsΒ1 integrinPoint mutationsNew adhesionsBinding sites
2011
Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer
Seong J, Ouyang M, Kim T, Sun J, Wen P, Lu S, Zhuo Y, Llewellyn N, Schlaepfer D, Guan J, Chien S, Wang Y. Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer. Nature Communications 2011, 2: 406. PMID: 21792185, PMCID: PMC3373894, DOI: 10.1038/ncomms1414.Peer-Reviewed Original ResearchConceptsFocal adhesion kinase activationFocal adhesion kinaseDetergent-resistant membranesMembrane microdomainsSubcellular localization of focal adhesion kinaseLocalization of focal adhesion kinaseSrc activationCell adhesion to extracellular matrix proteinsAdhesion to extracellular matrix proteinsDetergent-resistant membrane microdomainsPlatelet-derived growth factorResponse to different physiological stimuliFluorescence resonance energy transferExtracellular matrix proteinsFAK activationSubcellular localizationCellular processesSubcellular compartmentsResonance energy transferKinase activityPlasma membraneCell adhesionMatrix proteinsFRET responseMicrodomains
2010
Disruption of Laminin-Integrin-CD151-Focal Adhesion Kinase Axis Sensitizes Breast Cancer Cells to ErbB2 Antagonists
Yang XH, Flores LM, Li Q, Zhou P, Xu F, Krop IE, Hemler ME. Disruption of Laminin-Integrin-CD151-Focal Adhesion Kinase Axis Sensitizes Breast Cancer Cells to ErbB2 Antagonists. Cancer Research 2010, 70: 2256-2263. PMID: 20197472, PMCID: PMC3310185, DOI: 10.1158/0008-5472.can-09-4032.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntigens, CDAntineoplastic AgentsBreast NeoplasmsCell Adhesion MoleculesCell Line, TumorDrug SynergismEnzyme ActivationFocal Adhesion Protein-Tyrosine KinasesHumansIntegrin alpha3beta1Integrin alpha6beta4LapatinibProtein Kinase InhibitorsQuinazolinesReceptor, ErbB-2Signal TransductionTetraspanin 24TrastuzumabConceptsAnti-ErbB2 agentsBreast cancer cellsHuman ErbB2Cancer cellsSensitizes breast cancer cellsTetraspanin protein CD151Mammary tumor cellsFocal adhesion kinaseLaminin-5ErbB2 antagonistTrastuzumab treatmentBreast cancerLaminin-binding integrinsDrug resistanceTumor cellsCD151 knockdownLaminin-integrinErbB2TrastuzumabCancerCD151CellsTreatmentKnockdownAgents
2009
Focal adhesion kinase modulates activation of NF-κB by flow in endothelial cells
Petzold T, Orr AW, Hahn C, Jhaveri KA, Parsons JT, Schwartz MA. Focal adhesion kinase modulates activation of NF-κB by flow in endothelial cells. American Journal Of Physiology - Cell Physiology 2009, 297: c814-c822. PMID: 19587216, PMCID: PMC2770750, DOI: 10.1152/ajpcell.00226.2009.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell NucleusCells, CulturedEndothelial CellsEndothelium, VascularFocal Adhesion Protein-Tyrosine KinasesHydrogen PeroxideI-kappa B KinaseIntegrinsIntercellular Adhesion Molecule-1MiceNF-kappa BPhosphorylationProtein Transportrac GTP-Binding ProteinsReactive Oxygen SpeciesSignal TransductionStress, MechanicalTranscription Factor RelATumor Necrosis Factor-alphaConceptsFocal adhesion kinaseAdhesion kinaseNF-kappaBRac activationTranscriptional activityDependent genesEndothelial cellsIntegrin activationP65 NF-kappaB subunitDegradation of IkappaBReactive oxygen productionFluid shear stressNF-kappaB subunitsSerine 536Phosphorylation of p65Novel mechanismNF-kappaB activationKinaseNF-kappaB phosphorylationPhosphorylationActivationNF-κBOxygen productionHydrogen peroxideCells
2007
A Critical Role for TLR4 in the Pathogenesis of Necrotizing Enterocolitis by Modulating Intestinal Injury and Repair
Leaphart CL, Cavallo J, Gribar SC, Cetin S, Li J, Branca MF, Dubowski TD, Sodhi CP, Hackam DJ. A Critical Role for TLR4 in the Pathogenesis of Necrotizing Enterocolitis by Modulating Intestinal Injury and Repair. The Journal Of Immunology 2007, 179: 4808-4820. PMID: 17878380, DOI: 10.4049/jimmunol.179.7.4808.Peer-Reviewed Original ResearchConceptsDevelopment of NECNEC developmentTLR4 activationEnterocyte apoptosisEnterocyte migrationTLR4-mutant C3H/HeJ miceC3H/HeOuJ miceC3H/HeJ miceTranslocation of LPSExpression of TLR4Cause of deathMurine intestinal epitheliumFocal adhesion kinaseNEC severityCritical roleIntestinal injuryMucosal injuryPreterm infantsNecrotizing enterocolitisEnterocyte injuryInflamed intestineIntestinal healingGastrointestinal diseasesHeJ miceIntestinal repair
2006
Vitamin D regulates the phenotype of human breast cancer cells
Pendás-Franco N, González-Sancho J, Suárez Y, Aguilera O, Steinmeyer A, Gamallo C, Berciano MT, Lafarga M, Muñoz A. Vitamin D regulates the phenotype of human breast cancer cells. Differentiation 2006, 75: 193-207. PMID: 17288543, DOI: 10.1111/j.1432-0436.2006.00131.x.Peer-Reviewed Original ResearchConceptsSmooth muscle alpha-actinFocal adhesion kinaseBreast cancer cellsHuman breast cancer cellsCancer cellsP-cadherinFocal adhesion plaquesMDA-MB-453Muscle alpha-actinMesenchymal markers N-cadherinMDA-MB-468 cellsAdhesion kinasePlasma membraneAdhesion plaquesMDA-MB-453 cellsLarge cytoplasmic extensionsActin filamentsE-cadherin expressionCell adhesionCell typesN-cadherinAlpha-actinBreast cancer cell linesCancer cell linesLaser confocalModulation of Cell–Fibronectin Matrix Interactions during Tissue Repair
Midwood KS, Mao Y, Hsia HC, Valenick LV, Schwarzbauer JE. Modulation of Cell–Fibronectin Matrix Interactions during Tissue Repair. Journal Of Investigative Dermatology Symposium Proceedings 2006, 11: 73-78. PMID: 17069013, DOI: 10.1038/sj.jidsymp.5650005.Peer-Reviewed Original ResearchConceptsFocal adhesion kinaseExtracellular matrixAlpha 4 beta 1Fibronectin matrixActin stress fibersECM protein tenascinAlpha v beta 3Cell surface receptorsFibrin-fibronectin matrixOrganization of fibronectinAlpha 5 beta 1 integrin receptorBeta 3 integrinActin cytoskeletonBeta 1 integrin receptorsEnvironmental signalsMotile phenotypeTransmembrane proteoglycansAdhesion kinaseRho GTPaseRho signalingWound provisional matrixBeta 1Stress fibersIntegrin functionMultiple intracellular
2004
Coregulation of Fibronectin Signaling and Matrix Contraction by Tenascin-C and Syndecan-4
Midwood KS, Valenick LV, Hsia HC, Schwarzbauer JE. Coregulation of Fibronectin Signaling and Matrix Contraction by Tenascin-C and Syndecan-4. Molecular Biology Of The Cell 2004, 15: 5670-5677. PMID: 15483051, PMCID: PMC532045, DOI: 10.1091/mbc.e04-08-0759.Peer-Reviewed Original ResearchConceptsSyndecan-4 functionsSyndecan-4Actin stress fiber formationFocal adhesion kinaseMatrix contractionStress fiber formationExtracellular matrix proteinsEfficient tissue repairEffects of tenascinProvisional matrixTissue repairHeparan sulfate proteoglycanAdhesion kinaseCell spreadingSignaling pathwaysMatrix proteinsFibronectin signalingThree-dimensional fibrinExtracellular matrixFiber formationSulfate proteoglycanCell interactionsFibroblast morphologyTenascinFibroblast response
2003
Regulation of the intestinal epithelial response to cyclic strain by extracellular matrix proteins
Zhang J, Li W, Sanders MA, Sumpio BE, Asit P, Basson MD. Regulation of the intestinal epithelial response to cyclic strain by extracellular matrix proteins. The FASEB Journal 2003, 17: 1-22. PMID: 12626437, DOI: 10.1096/fj.02-0663fje.Peer-Reviewed Original ResearchMeSH KeywordsCaco-2 CellsCell AdhesionCell DivisionCell LineCollagen Type ICollagen Type IVEnzyme ActivationEpithelial CellsExtracellular Matrix ProteinsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansIntegrin alpha5Integrin alphaVIntestinal MucosaLamininMitogen-Activated Protein KinasesPhosphorylationProtein-Tyrosine KinasesStress, MechanicalConceptsExtracellular signal-regulated protein kinaseMatrix proteinsIntestinal epithelial responsesHuman intestinal epithelial proliferationSignal-regulated protein kinaseJun N-terminal kinaseFocal adhesion kinaseIntestinal epithelial biologyMatrix-dependent mannerN-terminal kinaseExtracellular matrix proteinsEpithelial responseCaco-2 proliferationCaco-2BBe cellsIntestinal epithelial proliferationAdhesion kinaseEpidermal growth factorProtein kinaseERK activationEpithelial biologyEpithelial cell proliferationIntegrin subunitsKinaseAnti-integrin antibodiesMEK blockadePlatelet–endothelial cell adhesion molecule-1 modulates endothelial migration through its immunoreceptor tyrosine-based inhibitory motif
Gratzinger D, Barreuther M, Madri JA. Platelet–endothelial cell adhesion molecule-1 modulates endothelial migration through its immunoreceptor tyrosine-based inhibitory motif. Biochemical And Biophysical Research Communications 2003, 301: 243-249. PMID: 12535670, DOI: 10.1016/s0006-291x(02)02982-0.Peer-Reviewed Original ResearchMeSH KeywordsAdherens JunctionsAmino Acid MotifsAnimalsCattleCell MovementCells, CulturedEndothelium, VascularEnzyme ActivationIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein BindingProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine PhosphatasesRecombinant Fusion ProteinsTyrosineConceptsSHP-2Tyrosine phosphatase SHP-2Endothelial migrationFocal contact componentsPlatelet endothelial cell adhesion molecule-1Phosphatase SHP-2Cell-cell junctionsImmunoreceptor tyrosine-based inhibitory motifCell-substrate adhesionFocal adhesion kinaseTyrosine-based inhibitory motifPECAM-1Endothelial cellsPECAM-1 phosphorylationSelective dephosphorylationAdhesion kinaseTyrosine phosphorylationAdhesion proteinsRecombinant proteinsCytoskeletal fractionCell adhesion molecule-1Coordinated migrationInhibitory motifPhosphorylationAdhesion molecule-1
2001
Focal Adhesion Kinase Activates Stat1 in Integrin-mediated Cell Migration and Adhesion*
Xie B, Zhao J, Kitagawa M, Durbin J, Madri J, Guan J, Fu X. Focal Adhesion Kinase Activates Stat1 in Integrin-mediated Cell Migration and Adhesion*. Journal Of Biological Chemistry 2001, 276: 19512-19523. PMID: 11278462, DOI: 10.1074/jbc.m009063200.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCell AdhesionCell LineCell MovementDNA-Binding ProteinsDose-Response Relationship, DrugEnzyme ActivationFibroblastsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGene DeletionGlutathione TransferaseHumansIntegrinsMicroscopy, FluorescenceMutagenesis, Site-DirectedMutationPhosphorylationPlasmidsPrecipitin TestsProtein BindingProtein Structure, TertiaryProtein-Tyrosine KinasesSignal TransductionSTAT1 Transcription FactorSTAT3 Transcription FactorTime FactorsTrans-ActivatorsTransfectionConceptsFocal adhesion kinaseCell adhesionCell migrationFAK-deficient cellsIntegrin/focal adhesion kinaseC-terminal deletionsAdhesion kinaseTerminal domainFAK localizationTranscription pathwayFocal contactsSignal transducerSTAT1PathwayRecent studiesAdhesionMigrationCellsKinaseIntegrinsSTAT3DeletionActivatorFirst timeActivationThe Integrin-Mediated Cyclic Strain-Induced Signaling Pathway in Vascular Endothelial Cells
Frangos S, Knox R, Yano Y, Chen E, Di Luozzo G, Chen A, Sumpio B. The Integrin-Mediated Cyclic Strain-Induced Signaling Pathway in Vascular Endothelial Cells. Endothelium 2001, 8: 1-10. PMID: 11409847, DOI: 10.3109/10623320109063153.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinase (MAPK) familyCytoplasmic protein kinaseProtein kinase familySignal transduction pathwaysFocal adhesion kinaseExtracellular matrix receptorsProcess of phosphorylationEndothelial cellsKinase familySignal transductionTranscription factorsAdhesion kinaseProtein kinaseTransduction pathwaysMatrix receptorsGene expressionTyrosine residuesSignaling pathwaysCyclic circumferential strainVascular endothelial cellsPathwayKinaseIntegrinsHemodynamic forcesVasculature resultsIntegrin and FAK-mediated MAPK activation is required for cyclic strain mitogenic effects in Caco-2 cells
Li W, Duzgun A, Sumpio B, Basson M. Integrin and FAK-mediated MAPK activation is required for cyclic strain mitogenic effects in Caco-2 cells. AJP Gastrointestinal And Liver Physiology 2001, 280: g75-g87. PMID: 11123200, DOI: 10.1152/ajpgi.2001.280.1.g75.Peer-Reviewed Original ResearchMeSH KeywordsCaco-2 CellsCell DivisionCell MovementCytoskeletal ProteinsEnzyme InhibitorsExtracellular MatrixFlavonoidsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGene Expression Regulation, EnzymologicHumansImidazolesIntegrinsIntestinesMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9Mitogen-Activated Protein KinasesNaphthalenesp38 Mitogen-Activated Protein KinasesPaxillinPhosphoproteinsPhosphorylationProtein-Tyrosine KinasesPyridinesStress, MechanicalTransfectionConceptsFocal adhesion kinaseMAPK extracellular signal-regulated kinaseCaco-2 cellsMitogen-activated protein kinase activationVitro kinase assaysProtein kinase activationSignal-regulated kinaseMitogenic effectProtein kinase C inhibitionBeta1 integrin subunitsCaco-2 proliferationKinase assaysAdhesion kinaseFAK activationERK signalsJNK1 activationKinase activationTerminal kinaseMAPK activationUpstream signalsC-JunFAK inhibitionP38 inhibitionIntegrin subunitsKinase
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