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J Biol Chem, Vol. 273, Issue 32, 19977-19981, August 7, 1998
From the Phagocytosis requires extension of F-actin-rich
pseudopods and is accompanied by membrane fusion events. Members of the
ARF family of GTPases are essential for many aspects of membrane
trafficking. To test a role for this family of proteins in Fc
A Requirement for ARF6 in Fc
Receptor-mediated
Phagocytosis in Macrophages
,,,
Departments of Medicine and Pharmacology,
Columbia University College of Physicians and Surgeons, New York,
New York 10032 and the § Laboratory of Cell Biology, NHLBI,
National Institutes of Health, Bethesda, Maryland 20892
receptor-mediated phagocytosis, we utilized the fungal metabolite
brefeldin A (BFA). The addition of 100 µM BFA to a
subclone of RAW 264.7 macrophages disrupted the appearance and function
of the Golgi apparatus as indicated by altered immunofluorescent
distribution of 
-COP and reduced efflux of BODIPY
C5-ceramide, a phospholipid that normally accumulates
in the Golgi apparatus. In contrast, BFA had no effect on phagocytosis
of IgG-coated erythrocytes. These results suggested that activation of
BFA-sensitive ARFs is not required for phagocytosis. ARF6 is unique
among members of the ARF family in that its membrane association is
unaffected by BFA. Expression of ARF6 mutants defective in either GTP
hydrolysis (Q67L) or binding (T27N) inhibited phagocytosis of
IgG-coated erythrocytes and attenuated the focal accumulation of
F-actin beneath the test particles. These results indicate a
requirement for ARF6 in Fc receptor-mediated phagocytosis and suggest that ARF6 is an important mediator of cytoskeletal alterations after Fc receptor activation.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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