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a phosphatidylinositol-3-kinase-dependent signal transition regulates arf1 and arf6 during fcγ receptor-mediated phagocytosisphosphatidylinositol-3-kinase-dependent信号过渡期间调节arf1和arf6 fcγ受体介导吞噬作用
PLoS BIOLOGY
A Phosphatidylinositol-3-Kinase-Dependent
Signal Transition Regulates ARF1 and ARF6
during Fcc Receptor-Mediated Phagocytosis
1 2 1,2*
Peter Beemiller , Adam D. Hoppe , Joel A. Swanson
1 Cellular and Molecular Biology Graduate Program, University of Michigan Medical School, Ann Arbor, Michigan, United States of America, 2 Department of Microbiology
and Immunology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America
Fcc receptor (FccR)–mediated phagocytosis of IgG-coated particles is regulated by 39-phosphoinositides (39PIs) and
several classes of small GTPases, including ARF6 from the ADP Ribosylation Factor subfamily. The insensitivity of
phagocytosis to brefeldin A (BFA), an inhibitor of certain ARF guanine nucleotide exchange factors (GEFs), previously
indicated that ARF1 did not participate in phagocytosis. In this study, we show that ARF1 was activated during FccR-
mediated phagocytosis and that blocking normal ARF1 cycling inhibited phagosome closure. We examined the
distributions and activation patterns of ARF6 and ARF1 during FccR-mediated phagocytosis using fluorescence
resonance energy transfer (FRET) stoichiometric microscopy of macrophages expressing CFP- or YFP-chimeras of ARF1,
ARF6, and a GTP-ARF-binding protein domain. Both GTPases were activated by BFA-insensitive factors at sites of
phagocytosis. ARF6 activation was restricted to the leading edge of the phagocytic cup, while ARF1 activation was
delayed and delocalized over the phagosome. Phagocytic cups formed after inhibition of PI 3-kinase (PI-3K) contained
persistently activated ARF6 and minimally activated ARF1. This indicates that a PI-3K-dependent signal transition
defines the sequence of ARF GTPase
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