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dc.contributor.authorSosa-Costa, Albertoes_ES
dc.contributor.authorIsern de Val, Soledades_ES
dc.contributor.authorSevilla-Movilla, Silviaes_ES
dc.contributor.authorBorgman, Kyra J. E.es_ES
dc.contributor.authorManzo, Carloes_ES
dc.contributor.authorTeixidó, Joaquínes_ES
dc.contributor.authorGarcia-Parajo, Maria F.es_ES
dc.date.accessioned2017-08-10T09:59:55Z-
dc.date.available2017-08-10T09:59:55Z-
dc.date.issued2016-09-30-
dc.identifier.citationThe Journal of Biological Chemistry 291 (40) 21053–21062 (2016)es_ES
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10261/154038-
dc.description11p.-8 fig.es_ES
dc.description.abstractChemokine stimulation of integrin α4β1-dependent T lymphocyte adhesion is a key step during lymphocyte trafficking. A central question regarding α4β1 function is how its lateral mobility and organization influence its affinity and avidity following cell stimulation with chemokines and/or ligands. Using single particle tracking and super-resolution imaging approaches, we explored the lateral mobility and spatial arrangement of individual α4β1 integrins on T cells exposed to different activating stimuli. We show that CXCL12 stimulation leads to rapid and transient α4β1 activation, measured by induction of the activation epitope recognized by the HUTS-21 anti-β1 antibody and by increased talin-β1 association. CXCL12-dependent α4β1 activation directly correlated with restricted lateral diffusion and integrin immobilization. Moreover, co-stimulation by CXCL12 together with soluble VCAM-1 potentiated integrin immobilization with a five-fold increase in immobile integrins as compared to unstimulated conditions. Our data indicate that docking by talin of the chemokine-activated α4β1 to the actin cytoskeleton favors integrin immobilization, which likely facilitates ligand interaction and increased adhesiveness. Super-resolution imaging showed that the nanoscale organization of high-affinity α4β1 remains unaffected following chemokine and/or ligand addition. Instead, newly activated α4β1 integrins organize on the cell membrane as independent units without joining pre-established integrin sites to contribute to cluster formation. Altogether, our results provide a rationale to understand how the spatiotemporal organization of activated α4β1 integrins regulates T lymphocyte adhesion.es_ES
dc.description.sponsorshipThis work was supported by Erasmus Mundus Doctorate Program Europhotonics Grant 159224-1-2009-1-FR-ERA MUNDUS-EMJD), Spanish Ministry of Economy and Competitiveness “Severo Ochoa” Programme for Centres of Excellence in R&D Grants SEV-2015–0522, FIS2014 –5617-R, SAF2014–53059-R, and RD12/0036/0061; Fundacio Privada CELLEX (Barcelona);HFSP Grant GA RGP0027/2012; and LaserLab Europe 4 Grant GA 654148.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyes_ES
dc.relationMINECO/ICTI2013-2016/SEV-2015-0522es_ES
dc.relationMINECO/ICTI2013-2016/FIS2014-5617-Res_ES
dc.relationMINECO/ICTI2013-2016/SAF2014-53059-Res_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccessen_EN
dc.subjectCell adhesiones_ES
dc.subjectCell migrationes_ES
dc.subjectIntegrines_ES
dc.subjectMembrane biophysicses_ES
dc.subjectMicroscopyes_ES
dc.subjectSingle particle analysises_ES
dc.titleLateral mobility and nanoscale spatial arrangement of chemokine-activated α4β1 integrins on T cellses_ES
dc.typeartículoes_ES
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M116.733709-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1074/jbc.M116.733709es_ES
dc.identifier.e-issn1083-351X-
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderLASERLAB-EUROPEes_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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