English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/212525
logo share SHARE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


RIAM-VASP Module Relays Integrin Complement Receptors in Outside-In Signaling Driving Particle Engulfment

AuthorsTorres-Gomez, Alvaro; Sanchez-Trincado, Jose Luis; Toribio, Víctor; Torres-Ruiz, Raul; Rodríguez-Perales, Sandra; Yáñez-Mó, María; Reche, Pedro A.; Cabañas, Carlos ; Lafuente, Esther M.
Issue Date8-May-2020
PublisherMultidisciplinary Digital Publishing Institute
CitationCells 9 (5): 1166 (2020)
AbstractThe phagocytic integrins and complement receptors &alpha;<sub>M</sub>&beta;<sub>2</sub>/CR3 and &alpha;<sub>X</sub>&beta;<sub>2</sub>/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 &beta;<sub>2</sub> 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.
Identifiersdoi: 10.3390/cells9051166
Appears in Collections:Colección MDPI
Files in This Item:
File Description SizeFormat 
cells-09-01166-v2.pdf3,46 MBAdobe PDFThumbnail
Show full item record
Review this work

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.