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dc.contributor.authorTorres-Gomez, Alvaro
dc.contributor.authorSanchez-Trincado, Jose Luis
dc.contributor.authorToribio, Víctor
dc.contributor.authorTorres-Ruiz, Raul
dc.contributor.authorRodriguez Perales, Sandra 
dc.contributor.authorReche, Pedro A
dc.contributor.authorYáñez-Mó, María
dc.contributor.authorCabañas, Carlos
dc.contributor.authorLafuente, Esther M
dc.identifier.citationCells . 2020;9(5):1166.es_ES
dc.description.abstractThe phagocytic integrins and complement receptors αMβ2/CR3 and αXβ2/CR4 are classically associated with the phagocytosis of iC3b-opsonized particles. The activation of this receptor is dependent on signals derived from other receptors (inside-out signaling) with the crucial involvement of the Rap1-RIAM-Talin-1 pathway. Here, we analyze the implication of RIAM and its binding partner VASP in the signaling events occurring downstream of β2 integrins (outside-in) during complement-mediated phagocytosis. To this end, we used HL-60 promyelocytic cell lines deficient in RIAM or VASP or overexpressing EGFP-tagged VASP to determine VASP dynamics at phagocytic cups. Our results indicate that RIAM-deficient HL-60 cells presented impaired particle internalization and altered integrin downstream signaling during complement-dependent phagocytosis. Similarly, VASP deficiency completely blocked phagocytosis, while VASP overexpression increased the random movement of phagocytic particles at the cell surface, with reduced internalization. Moreover, the recruitment of VASP to particle contact sites, amount of pSer157-VASP and formation of actin-rich phagocytic cups were dependent on RIAM expression. Our results suggested that RIAM worked as a relay for integrin complement receptors in outside-in signaling, coordinating integrin activation and cytoskeletal rearrangements via its interaction with VASP.es_ES
dc.description.sponsorshipThis work has been supported by Ministerio Espanol de Economia y Competitividad (MINECO) grants: SAF2016-77096-R (ELD and CC), BIO2014:54164-R (PAR), BIO2017-86500-R (MY-M), EI/MICIU EXPLORA BIO2017-91272-EXP & FEDER (PI17/02303) (S.R.-P). AT-G is supported by a predoctoral fellowship from MINECO, JLS-T is supported by a predoctoral fellowship from Universidad Complutense de Madrid, RT-R is supported by a postdoctoral fellowship from Asociacion Espanola Contra el Cancer (AECC).es_ES
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI) es_ES
dc.subject.meshPhagocytosis es_ES
dc.subject.meshSignal Transduction es_ES
dc.subject.meshActins es_ES
dc.subject.meshAdaptor Proteins, Signal Transducing es_ES
dc.subject.meshCell Adhesion Molecules es_ES
dc.subject.meshCell Membrane es_ES
dc.subject.meshComplement System Proteins es_ES
dc.subject.meshGene Knockdown Techniques es_ES
dc.subject.meshHL-60 Cells es_ES
dc.subject.meshHumans es_ES
dc.subject.meshIntegrins es_ES
dc.subject.meshManganese es_ES
dc.subject.meshMembrane Proteins es_ES
dc.subject.meshMicrofilament Proteins es_ES
dc.subject.meshPhosphoproteins es_ES
dc.subject.meshPhosphorylation es_ES
dc.subject.meshReceptors, Complement es_ES
dc.titleRIAM-VASP Module Relays Integrin Complement Receptors in Outside-In Signaling Driving Particle Engulfment.es_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.contributor.funderMinisterio de Economía y Competitividad (España) 
dc.contributor.funderComplutense University of Madrid (España) 
dc.contributor.funderAsociación Española Contra el Cáncer 
dc.contributor.funderUnión Europea. Comisión Europea 
dc.repisalud.orgCNIOCNIO::Unidades técnicas::Unidad de Citogenética Moleculares_ES
dc.rights.accessRightsopen accesses_ES
dc.relation.projectFISinfo:fis/Instituto de Salud Carlos III/Programa Estatal de Fomento de la Investigación Científica y Técnica de Excelencia/Subprograma Estatal de Generación de Conocimiento/PI17 - Proyectos de investigacion en salud (AES 2017). Modalidad proyectos en salud. (2017)/PI17/02303es_ES

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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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