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Vol. 18, Issue 3, 976-985, March 2007
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M
2-mediated Phagocytosis
*Centre for Molecular Microbiology and Infection and Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom; and Department of Biochemistry, University of Leicester, Leicester LE1 9HN, United Kingdom
Submitted September 13, 2006;
Revised December 13, 2006;
Accepted December 21, 2006
Monitoring Editor: Carole Parent
The cytoskeletal, actin-binding protein talin has been previously implicated in phagocytosis in Dictyostelium discoideum and mammalian phagocytes. However, its mechanism of action during internalization is not understood. Our data confirm that endogenous talin can occasionally be found at phagosomes forming around IgG- and C3bi-opsonized red blood cells in macrophages. Remarkably, talin knockdown specifically abrogates uptake through complement receptor 3 (CR3, CD11b/CD18, 
M
2 integrin) and not through the Fc 
receptor. We show that talin physically interacts with CR3/M2 and that this interaction involves the talin head domain and residues W747 and F754 in the 2 integrin cytoplasmic domain. The CR3/M2–talin head interaction controls not only talin recruitment to forming phagosomes but also CR3/M2 binding activity, both in macrophages and transfected fibroblasts. However, the talin head domain alone cannot support phagocytosis. Our results establish for the first time at least two distinct roles for talin during CR3/M2-mediated phagocytosis, most noticeably activation of the CR3/M2 receptor and phagocytic uptake.
Present address: Pathologie Infectieuse et Immunologie, Institut National de la Recherche Agronomique de Tours, 37380 Nouzilly, France.
Address correspondence to: Emmanuelle Caron (e.caron{at}imperial.ac.uk)
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