An essential function for the calcium-promoted Ras inactivator in Fcgamma receptor-mediated phagocytosis.
Fc receptor (FcR)-mediated phagocytosis requires activation of the Rho GTPases Cdc42 and Rac1, but how they are recruited to the FcR is unknown. Here we show that the calcium-promoted Ras inactivator (CAPRI), a Ras GTPase-activating protein, functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis. CAPRI-deficient macrophages had impaired FcgammaR-mediated phagocytosis and oxidative burst, as well as defective activation of Cdc42 and Rac1. CAPRI interacted constitutively with both Cdc42 and Rac1 and translocated to phagocytic cups during FcgammaR-mediated phagocytosis. CAPRI-deficient mice had an impaired innate immune response to bacterial infection. These results suggest that CAPRI provides a link between FcgammaR and Cdc42 and Rac1 and is essential for innate immune responses.
Duke Scholars
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- ras GTPase-Activating Proteins
- rac1 GTP-Binding Protein
- cdc42 GTP-Binding Protein
- Toll-Like Receptors
- Receptors, IgG
- Receptors, Cell Surface
- Phosphorylation
- Phagocytosis
- Molecular Sequence Data
- Mice, Knockout
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- ras GTPase-Activating Proteins
- rac1 GTP-Binding Protein
- cdc42 GTP-Binding Protein
- Toll-Like Receptors
- Receptors, IgG
- Receptors, Cell Surface
- Phosphorylation
- Phagocytosis
- Molecular Sequence Data
- Mice, Knockout