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Article

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

1
Department of Immunology, Ophthalmology and Otorhinolaryngology, School of Medicine, Universidad Complutense de Madrid, and Instituto (I+12), 28040 Madrid, Spain
2
Severo Ochoa Center for Molecular Biology (CSIC-UAM), 28049 Madrid, Spain
3
Departamento de Biología Molecular, Universidad Autónoma de Madrid (UAM) and Instituto de Investigación Sanitaria La Princesa (IIS-IP), 28049 Madrid, Spain
4
Molecular Cytogenetics and Genome Editing Unit, Human Cancer Genetics Program, Centro Nacional de Investigaciones Oncológicas (CNIO), 28029 Madrid, Spain
5
Josep Carreras Leukemia Research Institute and Department of Biomedicine, School of Medicine, University of Barcelona, 08007 Barcelona, Spain
*
Author to whom correspondence should be addressed.
Cells 2020, 9(5), 1166; https://doi.org/10.3390/cells9051166
Received: 1 April 2020 / Revised: 27 April 2020 / Accepted: 7 May 2020 / Published: 8 May 2020
(This article belongs to the Special Issue The Role of Integrins in Health and Disease)
The 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. View Full-Text
Keywords: phagocytosis; complement; CR3; CR4; Mac-1; β2 integrins; RIAM; VASP; outside-in phagocytosis; complement; CR3; CR4; Mac-1; β2 integrins; RIAM; VASP; outside-in
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MDPI and ACS Style

Torres-Gomez, A.; Sanchez-Trincado, J.L.; Toribio, V.; Torres-Ruiz, R.; Rodríguez-Perales, S.; Yáñez-Mó, M.; Reche, P.A.; Cabañas, C.; Lafuente, E.M. RIAM-VASP Module Relays Integrin Complement Receptors in Outside-In Signaling Driving Particle Engulfment. Cells 2020, 9, 1166. https://doi.org/10.3390/cells9051166

AMA Style

Torres-Gomez A, Sanchez-Trincado JL, Toribio V, Torres-Ruiz R, Rodríguez-Perales S, Yáñez-Mó M, Reche PA, Cabañas C, Lafuente EM. RIAM-VASP Module Relays Integrin Complement Receptors in Outside-In Signaling Driving Particle Engulfment. Cells. 2020; 9(5):1166. https://doi.org/10.3390/cells9051166

Chicago/Turabian Style

Torres-Gomez, Alvaro, Jose L. Sanchez-Trincado, Víctor Toribio, Raul Torres-Ruiz, Sandra Rodríguez-Perales, María Yáñez-Mó, Pedro A. Reche, Carlos Cabañas, and Esther M. Lafuente 2020. "RIAM-VASP Module Relays Integrin Complement Receptors in Outside-In Signaling Driving Particle Engulfment" Cells 9, no. 5: 1166. https://doi.org/10.3390/cells9051166

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