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Volume 272, Number 33,
Issue of August 15, 1997
pp. 20564-20571
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Trimeric G Proteins Control Exocytosis in Chromaffin Cells
Go REGULATES THE PERIPHERAL ACTIN NETWORK AND
CATECHOLAMINE SECRETION BY A MECHANISM INVOLVING THE SMALL
GTP-BINDING PROTEIN Rho
(Received for publication, February 26, 1997, and in revised form, May 27, 1997)
Stéphane
Gasman
,
Sylvette
Chasserot-Golaz
,
Michel R.
Popoff
,
Dominique
Aunis
and
Marie-France
Bader
From the Institut National de la Santé et de la Recherche
Médicale, U-338 Biologie de la Communication Cellulaire, 5 rue Blaise Pascal, 67084 Strasbourg Cedex, France and
Toxines Microbiennes, Institut Pasteur, 75724 Paris
Cedex 15, France
Besides having a role in signal transduction,
heterotrimeric G proteins may be involved in membrane trafficking
events. In chromaffin cells, Go is associated with
secretory organelles and its activation by mastoparan inhibits the
ATP-dependent priming of exocytosis. The effectors by which
Go controls exocytosis are currently unknown. The
subplasmalemmal actin network is one candidate, since it modulates
secretion by controlling the movement of secretory granules to the
plasma membrane. In streptolysin-O-permeabilized chromaffin cells,
activation of exocytosis produces disassembly of cortical actin
filaments. Mastoparan blocks the calcium-evoked disruption of cortical
actin, and this effect is specifically inhibited by antibodies against
G o and by a synthetic peptide corresponding to the
COOH-terminal domain of G o. Disruption of actin
filaments with cytochalasin E and Clostridium perfringens iota toxin partially reverses the mastoparan-induced inhibition of
secretion. Furthermore, the effects of mastoparan on cortical actin and
exocytosis are greatly reduced in cells treated with Clostridium
botulinum C3 exoenzyme, which specifically inactivates the small
G protein Rho. We propose that the control exerted by the
granule-associated Go on exocytosis may be related to
effects on the cortical actin network through a sequence of events
which eventually involves the participation of Rho.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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