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
G_o 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)

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, G_o is associated with secretory organelles and its activation by mastoparan inhibits the ATP-dependent priming of exocytosis. The effectors by which G_o 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 G_o on exocytosis may be related to effects on the cortical actin network through a sequence of events which eventually involves the participation of Rho.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				V. A. Tobin and M. Ludwig The role of the actin cytoskeleton in oxytocin and vasopressin release from rat supraoptic nucleus neurons J. Physiol., August 1, 2007; 582(3): 1337 - 1348. [Abstract] [Full Text] [PDF]

				C. Ehre, A. H. Rossi, L. H. Abdullah, K. De Pestel, S. Hill, J. C. Olsen, and C. W. Davis Barrier role of actin filaments in regulated mucin secretion from airway goblet cells Am J Physiol Cell Physiol, January 1, 2005; 288(1): C46 - C56. [Abstract] [Full Text] [PDF]

				S. Gasman, S. Chasserot-Golaz, M. Malacombe, M. Way, and M.-F. Bader Regulated Exocytosis in Neuroendocrine Cells: A Role for Subplasmalemmal Cdc42/N-WASP-induced Actin Filaments Mol. Biol. Cell, February 1, 2004; 15(2): 520 - 531. [Abstract] [Full Text] [PDF]

				K. Sakurada, H. Kato, H. Nagumo, H. Hiraoka, K. Furuya, T. Ikuhara, Y. Yamakita, K. Fukunaga, E. Miyamoto, F. Matsumura, et al. Synapsin I Is Phosphorylated at Ser603 by p21-activated Kinases (PAKs) in Vitro and in PC12 Cells Stimulated with Bradykinin J. Biol. Chem., November 15, 2002; 277(47): 45473 - 45479. [Abstract] [Full Text] [PDF]

				J. D. Kilts, H. S. Connery, E. G. Arrington, M. M. Lewis, C. P. Lawler, G. S. Oxford, K. L. O'Malley, R. D. Todd, B. L. Blake, D. E. Nichols, et al. Functional Selectivity of Dopamine Receptor Agonists. II. Actions of Dihydrexidine in D2L Receptor-Transfected MN9D Cells and Pituitary Lactotrophs J. Pharmacol. Exp. Ther., June 1, 2002; 301(3): 1179 - 1189. [Abstract] [Full Text] [PDF]

				E. Dermitzaki, A. Gravanis, M. Venihaki, C. Stournaras, and A. N. Margioris Opioids Suppress Basal and Nicotine-Induced Catecholamine Secretion Via a Stabilizing Effect on Actin Filaments Endocrinology, May 1, 2001; 142(5): 2022 - 2031. [Abstract] [Full Text]

				F. Doussau, S. Gasman, Y. Humeau, F. Vitiello, M. Popoff, P. Boquet, M.-F. Bader, and B. Poulain A Rho-related GTPase Is Involved in Ca2+-dependent Neurotransmitter Exocytosis J. Biol. Chem., March 10, 2000; 275(11): 7764 - 7770. [Abstract] [Full Text] [PDF]

				D. Brown Targeting of membrane transporters in renal epithelia: when cell biology meets physiology Am J Physiol Renal Physiol, February 1, 2000; 278(2): F192 - F201. [Abstract] [Full Text] [PDF]

				R. Aikawa, I. Komuro, T. Yamazaki, Y. Zou, S. Kudoh, W. Zhu, T. Kadowaki, and Y. Yazaki Rho Family Small G Proteins Play Critical Roles in Mechanical Stress–Induced Hypertrophic Responses in Cardiac Myocytes Circ. Res., March 5, 1999; 84(4): 458 - 466. [Abstract] [Full Text] [PDF]

				S Gasman, S Chasserot-Golaz, M. Popoff, D Aunis, and M. Bader Involvement of Rho GTPases in calcium-regulated exocytosis from adrenal chromaffin cells J. Cell Sci., January 12, 1999; 112(24): 4763 - 4771. [Abstract] [PDF]

				M Kreft, S Gasman, S Chasserot-Golaz, V Kuster, M Rupnik, S. Sikdar, M Bader, and R Zorec The heterotrimeric Gi(3) protein acts in slow but not in fast exocytosis of rat melanotrophs J. Cell Sci., January 11, 1999; 112(22): 4143 - 4150. [Abstract] [PDF]

				W. E. McIntire, J. Dingus, K. L. Schey, and J. D. Hildebrandt Characterization of the Major Bovine Brain Go alpha  Isoforms. MAPPING THE STRUCTURAL DIFFERENCES BETWEEN THE alpha  SUBUNIT ISOFORMS IDENTIFIES A VARIABLE REGION OF THE PROTEIN INVOLVED IN RECEPTOR INTERACTIONS J. Biol. Chem., December 11, 1998; 273(50): 33135 - 33141. [Abstract] [Full Text] [PDF]

				S. Gasman, S. Chasserot-Golaz, P. Hubert, D. Aunis, and M.-F. Bader Identification of a Potential Effector Pathway for the Trimeric Go Protein Associated with Secretory Granules. Go STIMULATES A GRANULE-BOUND PHOSPHATIDYLINOSITOL 4-KINASE BY ACTIVATING RhoA IN CHROMAFFIN CELLS J. Biol. Chem., July 3, 1998; 273(27): 16913 - 16920. [Abstract] [Full Text] [PDF]

				A.-S. Caumont, M.-C. Galas, N. Vitale, D. Aunis, and M.-F. Bader Regulated Exocytosis in Chromaffin Cells. TRANSLOCATION OF ARF6 STIMULATES A PLASMA MEMBRANE-ASSOCIATED PHOSPHOLIPASE D J. Biol. Chem., January 16, 1998; 273(3): 1373 - 1379. [Abstract] [Full Text] [PDF]

				A. Harada, B. Furuta, K.-i. Takeuchi, M. Itakura, M. Takahashi, and M. Umeda Nadrin, a Novel Neuron-specific GTPase-activating Protein Involved in Regulated Exocytosis J. Biol. Chem., November 17, 2000; 275(47): 36885 - 36891. [Abstract] [Full Text] [PDF]

				E. Klussmann, G. Tamma, D. Lorenz, B. Wiesner, K. Maric, F. Hofmann, K. Aktories, G. Valenti, and W. Rosenthal An Inhibitory Role of Rho in the Vasopressin-mediated Translocation of Aquaporin-2 into Cell Membranes of Renal Principal Cells J. Biol. Chem., June 1, 2001; 276(23): 20451 - 20457. [Abstract] [Full Text] [PDF]