Journal
JOURNAL OF LEUKOCYTE BIOLOGY
Volume 76, Issue 6, Pages 1093-1103Publisher
WILEY
DOI: 10.1189/jlb.0804439
Keywords
macrophage; actin; PI-3 kinase; rac; Cdc42
Categories
Funding
- NIAID NIH HHS [AI53652, R01 AI035950, R01 AI035950-11, AI35950] Funding Source: Medline
- NIGMS NIH HHS [T32 GM145304] Funding Source: Medline
Ask authors/readers for more resources
Phagocytosis by macrophages can be initiated by Fegamma receptors (FcR) in membranes that bind to Fc regions of immunoglobulin G (IgG). Activated Felt transduce signals to cytoplasm, which regulate the internalization of IgG-coated particles into plasma membrane-derived vacuoles, phagosomes. Particles internalized by phagocytosis are much larger than FcR, which prompts questions of if and how the receptors are coordinated with each other. FcR-mediated signal transduction entails recruitment of proteins from cytoplasm to the receptor, largely via protein phosphorylation. These FcR signaling complexes then activate proteins that regulate actin, myosin, membrane fusion, and the production of reactive oxygen intermediates. Recent fluorescence microscopic studies of phagocytosis in macrophages indicate that signaling by FeR occurs as a sequence of distinct stages, evident in the spatial and temporal patterns of phosphoinositides, protein kinase C, and Rho-family GTPase activation on forming phagosomes. The coordination of these stages may be regulated by lipids or lipid-anchored proteins, which diffuse away from FcR complexes. Lateral diffusion of FcR-derived signals could integrate FcR-dependent responses over large areas of membrane in the forming phagosome.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available