2020
Cell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy
Amraei R, Alwani T, Ho R, Aryan Z, Wang S, Rahimi N. Cell adhesion molecule IGPR-1 activates AMPK connecting cell adhesion to autophagy. Journal Of Biological Chemistry 2020, 295: 16691-16699. PMID: 32978258, PMCID: PMC7864065, DOI: 10.1074/jbc.ra120.014790.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAMP-Activated Protein KinasesAnimalsAutophagyAutophagy-Related Protein-1 HomologBeclin-1CD28 AntigensCell AdhesionHEK293 CellsHumansI-kappa B KinaseIntracellular Signaling Peptides and ProteinsLipopolysaccharidesMicroscopy, FluorescenceMicrotubule-Associated ProteinsPhosphorylationPrimatesRNA, Guide, KinetoplastidaSirolimusSubstrate SpecificityConceptsIGPR-1Cell adhesionCell adhesion molecule IGPR-1Proline-rich receptor-1Serine/threonine kinaseKey serine/threonine kinaseAmino acid starvationBeclin-1Phosphorylation of AMPThreonine kinaseAutophagy stimuliKinase assaysLC3-II levelsCellular stressNutrient deprivationProtein kinaseCell adhesion moleculeProtein ULK1IκB kinase βEndothelial barrier functionKinase βCellular assaysPhosphorylationSubsequent activationCell detachment
2011
Effects of integrin-mediated cell adhesion on plasma membrane lipid raft components and signaling
Norambuena A, Schwartz MA. Effects of integrin-mediated cell adhesion on plasma membrane lipid raft components and signaling. Molecular Biology Of The Cell 2011, 22: 3456-3464. PMID: 21795400, PMCID: PMC3172269, DOI: 10.1091/mbc.e11-04-0361.Peer-Reviewed Original ResearchConceptsLipid raft componentsRaft componentsLipid raftsCyclic adenosine monophosphateCell detachmentCell adhesionLipid raft markersGlycosylphosphatidylinositol-linked proteinsRaft associationRaft markersRho GTPasesNonraft fractionsDetachment of cellsElevation of cAMPStudy of integrinsTermination of growthPlasma membraneH-RasAnchorage dependenceKey defenseCell growthFlotillin2Sucrose gradientsCancer metastasisLipid tails
2009
RalA-Exocyst Complex Regulates Integrin-Dependent Membrane Raft Exocytosis and Growth Signaling
Balasubramanian N, Meier JA, Scott DW, Norambuena A, White MA, Schwartz MA. RalA-Exocyst Complex Regulates Integrin-Dependent Membrane Raft Exocytosis and Growth Signaling. Current Biology 2009, 20: 75-79. PMID: 20005108, PMCID: PMC2822103, DOI: 10.1016/j.cub.2009.11.016.Peer-Reviewed Original ResearchConceptsPlasma membraneRecycling endosomesGrowth signalingActivation of Arf6Small GTPase RalACaveolin-dependent internalizationLipid raft microdomainsAnchorage-independent growthEffects of integrinsExocyst complexActive RalARaft microdomainsMembrane raftsRaft markersIntegrin signalingPancreatic cancer cellsRalAAnchorage dependenceAnchorage independenceCell growthSignalingCell detachmentCancer cellsEndosomesExocytosis
2005
Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization
del Pozo MA, Balasubramanian N, Alderson NB, Kiosses WB, Grande-García A, Anderson RG, Schwartz MA. Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization. Nature Cell Biology 2005, 7: 901-908. PMID: 16113676, PMCID: PMC1351395, DOI: 10.1038/ncb1293.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaveolaeCaveolin 1CaveolinsCell AdhesionCell ProliferationDynamin IIEndocytosisExtracellular MatrixExtracellular Signal-Regulated MAP KinasesFocal AdhesionsIntegrinsMembrane MicrodomainsMiceMice, KnockoutMicroscopy, Electron, TransmissionNeoplasm InvasivenessNeoplasmsNIH 3T3 CellsPhosphatidylinositol 3-KinasesPhosphorylationrac GTP-Binding ProteinsConceptsCaveolin-1Cholesterol-enriched membrane microdomainsPhosphatidylinositol-3-OH kinaseCell detachmentNovel molecular mechanismCholesterol-rich domainsInhibition of ERKMembrane microdomainsFocal adhesionsDynamin 2Plasma membraneMolecular mechanismsTumor suppressionTyr-14Multiple pathwaysNormal cellsInternalizationERKRacPathwayCaveolaeKinasePhosphorylationAdhesionMicrodomains
2004
Integrins Regulate Rac Targeting by Internalization of Membrane Domains
del Pozo MA, Alderson NB, Kiosses WB, Chiang HH, Anderson RG, Schwartz MA. Integrins Regulate Rac Targeting by Internalization of Membrane Domains. Science 2004, 303: 839-842. PMID: 14764880, DOI: 10.1126/science.1092571.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCell AdhesionCell LineCell MembraneCells, CulturedCholera ToxinCholesterolG(M1) GangliosideGlycosylphosphatidylinositolsGuanosine TriphosphateHumansIntegrin beta1IntegrinsLiposomesMembrane MicrodomainsMiceNIH 3T3 Cellsrac1 GTP-Binding ProteinRatsRecombinant Fusion ProteinsSignal TransductionTransfectionConceptsMembrane domainsLipid raftsLipid raft markersPlasma membrane cholesterolCholesterol-rich membranesCell plasma membraneMembrane targetingAdhesion of cellsSmall GTPRaft markersIntegrin signalsPlasma membraneDownstream effectorsEffector activationMembrane lipidsMembrane cholesterolAnchorage-dependent cellsExtracellular matrixCell detachmentNonadherent cellsInternalizationRaftsCellsTargetingMembrane
2001
Pseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair
Geiser T, Kazmierczak B, Garrity‐Ryan L, Matthay M, Engel J. Pseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair. Cellular Microbiology 2001, 3: 223-236. PMID: 11298646, DOI: 10.1046/j.1462-5822.2001.00107.x.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsEpithelial wound repairPseudomonas aeruginosa ExoTRho family GTPasesWound repairPathogen Pseudomonas aeruginosaNosocomial pathogen Pseudomonas aeruginosaP. aeruginosa internalizationEpithelial cellsP. aeruginosaGAP domainGAP activityBacterial proteinsCell roundingCytoskeleton collapseLung epithelial wound repairExoTCell detachmentVivo virulenceProteinEpithelial tissue damageImmune effector cellsLocal host defenseIntact epithelial barrierHost defense
2000
Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β*
Baron V, Schwartz M. Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β*. Journal Of Biological Chemistry 2000, 275: 39318-39323. PMID: 11007771, DOI: 10.1074/jbc.m003618200.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsBlotting, WesternCell AdhesionCell DivisionCell LineCells, CulturedCysteine EndopeptidasesDose-Response Relationship, DrugDown-RegulationDynaminsEmbryo, MammalianEnzyme InhibitorsFibroblastsFibronectinsGTP PhosphohydrolasesHumansLigandsLysosomesMiceMultienzyme ComplexesPhosphorylationProteasome Endopeptidase ComplexProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth FactorTemperatureTime FactorsTrypsinTyrphostinsUbiquitinsConceptsUbiquitin-dependent pathwayIntegrin-mediated adhesionPlatelet-derived growth factor receptor βPlatelet-derived growth factor receptor betaTyrosine kinase activityGrowth factor receptor βGrowth factor receptor betaProteasome pathwayDetachment of cellsReceptor autophosphorylationKinase activityCellular desensitizationPrimary fibroblastsExtracellular matrixCell detachmentAutophosphorylationProtein levelsCell linesPDGFGrowth factorReceptor betaReceptor βCellsPathwayRecent studies
1996
Role of neuron-glial junctional domain proteins in the maintenance and termination of neuronal migration across the embryonic cerebral wall
Anton E, Cameron R, Rakic P. Role of neuron-glial junctional domain proteins in the maintenance and termination of neuronal migration across the embryonic cerebral wall. Journal Of Neuroscience 1996, 16: 2283-2293. PMID: 8601808, PMCID: PMC6578523, DOI: 10.1523/jneurosci.16-07-02283.1996.Peer-Reviewed Original ResearchConceptsEmbryonic cerebral wallCerebral wallNeuronal migrationCerebral cortexNeuronal migratory pathwayRadial glial cell processesRadial glial fibersGlial cell processesNormal neuronal migrationCortical plateSlice preparationAntibody exposureGlial fibersMarginal zone regionsMonoclonal antibodiesAntibodiesNeuronsCortexCell substratesMarginal zonePolyclonal antiserumMicrotubular organizationCell processesMigratory pathwaysCell detachmentA cleavage-site-directed inhibitor of interleukin-1β-converting enzyme-like proteases inhibits apoptosis in primary cultures of rat hepatocytes
Kelvin C, INAYAT-HUSSAIN S, COUET C, COHEN G. A cleavage-site-directed inhibitor of interleukin-1β-converting enzyme-like proteases inhibits apoptosis in primary cultures of rat hepatocytes. Biochemical Journal 1996, 314: 27-32. PMID: 8660294, PMCID: PMC1217036, DOI: 10.1042/bj3140027.Peer-Reviewed Original ResearchConceptsEnzyme-like proteasesInterleukin-1beta-converting enzyme-like proteasesChromatin condensationConventional gel electrophoresisDNA cleavageCell detachmentGrowth factor beta1Gel electrophoresisPrimary hepatocytesApoptosisProteasePrimary culturesRat hepatocytesLiver apoptosisInhibitorsStaurosporineHepatocytesEnzyme
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