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Vol. 13, Issue 2, 402-411, February 2002
Receptor-mediated
Phagocytosis in Macrophages
and
*Department of Microbiology and Immunology, University of Michigan
Medical School, Ann Arbor, Michigan 48109-0620; and
Particle ingestion by phagocytosis results from sequential
rearrangements of the actin cytoskeleton and overlying membrane. To
assemble a chronology of molecular events during phagosome formation
and to examine the contributions of phosphoinositide 3-kinase (PI
3-kinase) to these dynamics, a method was developed for synchronizing
FcDepartments of Cell Biology and Immunology, Scripps
Research Institute, La Jolla, California 92037
receptor-mediated phagocytosis by murine macrophages.
Erythrocytes opsonized with complement component C3bi were bound to
macrophages at 37°C, a condition that does not favor particle
phagocytosis. Addition of soluble anti-erythrocyte IgG resulted in
rapid opsonization of the bound erythrocytes, followed by their
immediate internalization via phagocytosis. Cellular content of
F-actin, as measured by binding of rhodamine-phalloidin, increased
transiently during phagocytosis, and this increase was not diminished
by inhibitors of PI 3-kinase. Immunofluorescence localization of
myosins in macrophages fixed at various times during phagocytosis
indicated that myosins II and IXb were concentrated in early
phagosomes, myosin IC increased later, and myosin V appeared after
phagosome closure. Other cytoskeletal proteins showed similar variations in the timing of their appearance in phagosomes. The PI
3-kinase inhibitor wortmannin did not change the dynamics of PI
3-kinase or ezrin localization but prevented the loss of PAK1 from
phagosomes. These results suggest that PI 3-kinase deactivates PAK1,
and that this may be needed for phagosome closure.
Online version of this article contains video material for Figure
2. Online version is available at www.molbiolcell.org.
Corresponding author. E-mail address:
jswan{at}umich.edu.
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