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A specific role for ADP-ribosylation factors (ARFs) in in
vitro endosome-endosome fusion has been proposed (Lenhard, J. M.,
Kahn, R. A., and Stahl, P. D.(1992) J. Biol. Chem. 267,
13047-13052). However, in vivo studies have failed to
support a function for ARFs in the endocytic pathway, since an
antagonist of ARF activities, brefeldin A, does not interfere with
receptor internalization (Schonhorn, J. E., and Wessling-Resnick,
M.(1994) Mol. Cell. Biochem. 135, 159-164). This
controversy surrounding the exact function of ARF in endocytic vesicle
traffic prompted us to critically re-examine the involvement of ARFs in
cell-free endosome fusion. Cytosol depleted of ARF activity was capable
of supporting in vitro endocytic vesicle fusion but failed to
support inhibition of this reaction in the presence of guanosine
5`-3-O-(thio)triphosphate (GTP
Volume 270,
Number 23,
Issue of June 9, pp. 13693-13697, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
S Inhibition of Fusion
S). Addition of purified
ARF1 restored the ability of the ARF-depleted cytosol to inhibit
endosome fusion when incubated with GTP
S. Both endocytic vesicle
fusion and the GTP
S-mediated inhibition of vesicle fusion were
unaffected by brefeldin A. Moreover, the ATP requirement and kinetics
of cell-free fusion are not altered by brefeldin A or depletion of
cytosolic ARFs. These results suggest that cytosolic ARFs are not
necessary for endosomal vesicle fusion in vitro but are
responsible for inhibition of fusion in the presence of GTP
S and
cytosolic factors in a brefeldin A-resistant manner.
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