2025
CFTR dictates monocyte adhesion by facilitating integrin clustering but not activation
Younis D, Marosvari M, Liu W, Pulikkot S, Cao Z, Zhou B, Vella A, McArdle S, Hu L, Chen Y, Gan W, Yu J, Bruscia E, Fan Z. CFTR dictates monocyte adhesion by facilitating integrin clustering but not activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2412717122. PMID: 39813254, PMCID: PMC11760921, DOI: 10.1073/pnas.2412717122.Peer-Reviewed Original ResearchConceptsIntegrin clusteringCF transmembrane conductance regulatorCystic fibrosisAdhesion defectsPathogenesis of cystic fibrosisClinically relevant disease modelsMembrane recruitmentTransmembrane conductance regulatorIntegrin activationTherapeutic strategy designRelevant disease modelsIntegrinCF monocytesCell adhesionMonocyte dysfunctionPatients' monocytesTissue infectionsConductance regulatorSuperresolution microscopyCortex formationLeukocyte-dependent inflammationInflammatory pathogenesisLeukocyte adhesionMonocytesInflammationNanoscopy reveals integrin clustering reliant on kindlin-3 but not talin-1
Wu Y, Cao Z, Liu W, Cahoon J, Wang K, Wang P, Hu L, Chen Y, Moser M, Vella A, Ley K, Wen L, Fan Z. Nanoscopy reveals integrin clustering reliant on kindlin-3 but not talin-1. Cell Communication And Signaling 2025, 23: 12. PMID: 39773732, PMCID: PMC11707915, DOI: 10.1186/s12964-024-02024-8.Peer-Reviewed Original Research
2024
Conformational response of αIIbβ3 and αVβ3 integrins to force
Kolasangiani R, Farzanian K, Chen Y, Schwartz M, Bidone T. Conformational response of αIIbβ3 and αVβ3 integrins to force. Structure 2024, 33: 289-299.e4. PMID: 39706199, DOI: 10.1016/j.str.2024.11.016.Peer-Reviewed Original ResearchConceptsBind similar ligandsExtended conformationAvb3 integrinCellular mechanosensingAdhesion receptorsSubunit domainsCell mechanosensingPlasma membraneIntegrinMechanical signalsAll-atom simulationsSingle molecule measurementsConformational responseSubunitMechanosensingStructural dynamicsSolid tissuesCellsMolecule measurementsConformationAvb3Circulating plateletsEquivalent levelMembraneRenal Angptl4 is a key fibrogenic molecule in progressive diabetic kidney disease
Srivastava S, Zhou H, Shenoi R, Morris M, Lainez-Mas B, Goedeke L, Rajendran B, Setia O, Aryal B, Kanasaki K, Koya D, Inoki K, Dardik A, Bell T, Fernández-Hernando C, Shulman G, Goodwin J. Renal Angptl4 is a key fibrogenic molecule in progressive diabetic kidney disease. Science Advances 2024, 10: eadn6068. PMID: 39630889, PMCID: PMC11616692, DOI: 10.1126/sciadv.adn6068.Peer-Reviewed Original ResearchConceptsAngiopoietin-like 4Diabetic kidney diseaseIntegrin B1Fibrogenic moleculesMutant miceSTING pathway activationIncreased fatty acid oxidationProgressive diabetic kidney diseaseDiabetic kidneyKidney diseaseReduced epithelial-to-mesenchymal transitionEpithelial-to-mesenchymal transitionFatty acid oxidationExpression of pro-inflammatory cytokinesTargeted pharmacological therapiesGene expressionMitochondrial damageEndothelial-to-mesenchymal transitionPro-inflammatory cytokinesPathway activationPharmacological therapyControl miceIntegrinAcid oxidationFibrogenic phenotypeLive imaging of Fibronectin 1a-mNeonGreen and Fibronectin 1b-mCherry knock-in alleles during early zebrafish development
Jülich D, Holley S. Live imaging of Fibronectin 1a-mNeonGreen and Fibronectin 1b-mCherry knock-in alleles during early zebrafish development. Cells And Development 2024, 177: 203900. PMID: 38218338, PMCID: PMC10947920, DOI: 10.1016/j.cdev.2024.203900.Peer-Reviewed Original ResearchKnock-in alleleECM fibersLoss of function phenotypesGenetic complementation experimentsAdhesion receptor familyComplementation experimentsDouble mutantLive in vivo imagingExtracellular matrix glycoproteinFibronectin matrixPosterior hindgutPresomitic mesodermZebrafish developmentExpression patternsMRNA injectionIntegrinLive imagingCross-regulationAllelesFibronectinReceptor familyParaxial mesodermCo-localizationExtracellular matrixMutants
2006
The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein*
Mazurov D, Heidecker G, Derse D. The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein*. Journal Of Biological Chemistry 2006, 282: 3896-3903. PMID: 17166843, DOI: 10.1074/jbc.m607322200.Peer-Reviewed Original ResearchConceptsTetraspanin-enriched microdomainsC-terminusN-terminusTetraspanin superfamily proteinsSite-directed mutationsMembrane protein complexesExtracellular loopCytoplasmic N-terminusHTLV-1T cell adhesionIntegrin functionPalmitoylated cysteinesSuperfamily proteinsProtein complexesTetraspanin CD82Cytoplasmic facePlasma membraneHTLV-1 GagColocalization approachesAmino acidsCD82IntegrinTetraspaninMutationsCD81
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