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Vol. 273, Issue 3, 1373-1379, January 16, 1998
From the The ADP-ribosylation factor (ARF) GTP-binding
proteins have been implicated in a wide range of vesicle transport and
fusion steps along the secretory pathway. In chromaffin cells, ARF6 is specifically associated with the membrane of secretory chromaffin granules. Since ARF6 is an established regulator of phospholipase D
(PLD), we have examined the intracellular distribution of ARF6 and PLD
activity in resting and stimulated chromaffin cells. We found that
stimulation of intact chromaffin cells or direct elevation of cytosolic
calcium in permeabilized cells triggered the rapid translocation of
ARF6 from secretory granules to the plasma membrane and the concomitant
activation of PLD in the plasma membrane. To probe the existence of an
ARF6-dependent PLD in chromaffin cells, we measured the PLD
activity in purified plasma membranes. PLD could be activated by a
nonhydrolyzable analogue of GTP and by recombinant myristoylated ARF6
and inhibited by specific anti-ARF6 antibodies. Furthermore, a
synthetic myristoylated peptide corresponding to the N-terminal domain
of ARF6 inhibited both PLD activity and catecholamine secretion in
calcium-stimulated chromaffin cells. The possibility that ARF6
participates in the exocytotic reaction by controlling a plasma
membrane-bound PLD and thereby generating fusogenic lipids at the
exocytotic sites is discussed.
Regulated Exocytosis in Chromaffin Cells
TRANSLOCATION OF ARF6 STIMULATES A PLASMA MEMBRANE-ASSOCIATED
PHOSPHOLIPASE D
,,, and
INSERM, U-338 Biologie de la Communication
Cellulaire, 5 rue Blaise Pascal, 67084 Strasbourg Cedex, France and
§ Pulmonary-Critical Care Medicine Branch, NHLBI, National
Institutes of Health, Bethesda, Maryland 20814
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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