Scinderin and cortical F-actin are components of the secretory machinery

Canadian Journal of Physiology and Pharmacology

Volumn 77, Issue 9, 1999, Pages 660-671

  Trifaro J M ^a  

^a UNIVERSITY OF OTTAWA   (Canada)

Author keywords

Chromaffin cell; Cytoskeleton; Exocytosis; F actin; Scinderin

Indexed keywords

F ACTIN; PROTEIN; SCINDERIN; UNCLASSIFIED DRUG;

CHROMAFFIN CELL; CONFERENCE PAPER; CYTOSKELETON; EXOCYTOSIS; MOLECULAR DYNAMICS; NEUROTRANSMITTER RELEASE; PRIORITY JOURNAL; PROTEIN LOCALIZATION; REGULATORY MECHANISM;

EID: 0032739451     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y99-074     Document Type: Conference Paper

References (43)

1. Alvarez de Toledo, G., Fernández-Chacón, R., and Fernández, J.M. 1993. Release of secretory products during transient vesicle fusion. Nature (London), 363: 554-557.
2. Aunis, D., and Perrin, D. 1984. Chromaffin granule membrane - F-actin interactions and spectrin-like protein of subcellular organelles: a possible relationship. J. Neurochem. 42: 1558-1569.
3. Bittner, M.A., and Holz, R.W. 1992. Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components. J. Biol. Chem. 267: 16219-16225.
4. Bommert, K., Charlton, M.P., DeBello, W.M., Chin, G.J., Betz, H., and Augustine, G.J. 1993. Inhibition of neurotransmitter release by C 2-domain peptides implicates synaptotagmin in exocytosis. Nature (London), 363: 163-165.
5. Burgoyne, R.D., Geisow, M.J., and Barron, J. 1982. Dissection of stages in exocytosis in the adrenal chromaffin cells with use of trifluoperazine. Proc. R. Soc. London Ser. B, 216: 111-115.
6. Burgoyne, R.D., Morgan, A., and O'Sullivan, A.J. 1989. The control of cytoskeletal actin and exocytosis in intact and permeabilized adrenal chromaffin cells: role of calcium and protein kinase C. Cell. Signalling, 1: 323-334.
7. Cheek, T.R., and Burgoyne, R.D. 1986. Nicotine-evoked disassembly of cortical actin filaments in adrenal chromaffin cells. FEBS Lett. 207: 110-114.
8. Cheek, T.R., and Burgoyne, R.D. 1991. Cytoskeleton in secretion and neurotransmitter release. In The neuronal cytoskeleton. Edited by R.D. Burgoyne. Wiley-Liss, New York. pp. 309-329.
9. Douglas, W.W. 1968. Stimulus-secretion coupling: the concept and clues from chromaffin and other cells. Br. J. Pharmacol. 34: 451-474.
10. Douglas, W.W., and Rubin, R.P. 1961. The role of calcium in the secretory response of the adrenal medulla to acetylcholine. J. Physiol. (London), 159: 40-57.
11. Fujita, T., and Kobayashi, T. 1979. Current views on the paraneurone concept. Trends Neurosci. 2: 27-30.
12. Harvey, D.G., and MacIntoch, F.C. 1940. Calcium and synaptic transmission in a sympathetic ganglion. J. Physiol. (London), 97: 408-418.
13. Heinemann, C., von Rüden, L., Chow, R.H., and Neher, E. 1993. A two-step model of secretion control in neuroendocrine cells. Pfluegers Arch. Eur. J. Physiol. 424: 105-112.
14. Houssay, B.A., and Molinelli, E.A. 1928. Excitabilité des fibres adrénalino-sécrétories due neuf grand splanchnique: fréquences, seuil et optimum des stimulus: rôle de l'ion calcium. C.R. Seances Soc. Biol. Ses Fil. 99: 172-174.
15. Jockush, B.M., Burger, M.M., Da Prada, M., Richards, J.G., Chaponnier, C., and Gabbiani, G. 1977. a-Actinin attaches to membranes of secretory vesicles. Nature (London), 270: 628-629.
16. Kondo, H., Wolosewick, J.J., and Pappas, G.D. 1982. The microtrabecular lattice of the adrenal medulla revealed by polyethylene glycol embedding and stereo electron microscopy. J. Neurosci. 2: 57-65.
17. Lee, R.W.H., and Trifaró, J.-M. 1981. Characterization of anti-actin antibodies and their use in immunocytochemical studies on the localization of actin in adrenal chromaffin cells in culture. Neuroscience, 6: 2087-2108.
18. 2+-dependent F-actin severing proteins. Mol. Cell. Biochem. 141: 153-165.
19. Marcu, M.G., Zhang, L., Nau-Staudt, K., and Trifaró, J.-M. 1996. Recombinant scinderin, an F-actin severing protein, increases calcium-induced release of serotonin from permeabilized platelets, an effect blocked by two scinderin-derived actin-binding peptides and phosphatidylinositol 4,5-bisphosphate. Blood, 87: 20-24.
20. Marcu, M.G., Zhang, L., Elzagallaai, A., and Trifaró, J.-M. 1998. Localization by segmented deletion analysis and functional characterization of a third actin-binding site in domain 5 of scinderin. J. Biol. Chem. 273: 3661-3668.
21. Nakata, T., and Hirokawa, N. 1992. Organization of cortical cytoskeleton in cultured chromaffin cells and involvement in secretion as revealed by quick-freeze, deep-etching and double-label immunoelectron microscopy. J. Neurosci. 12: 2186-2197.
22. Neher, E., and Zucker, R.S. 1993. Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron, 10: 21-30.
23. Orci, L., Gabbay, K.H., and Malaisse, W.J. 1972. Pancreatic beta-cell web: its possible role in insulin secretion. Science (Washington, D.C.), 175: 1128-1130.
24. Parsons, T.D., Coorssen, J.R., Horstmann, H., and Almers, W. 1995. Docked granules, the exocytotic burst, and the need for ATP hydrolysis in endocrine cells. Neuron, 15: 1085-1096.
25. Popov, S.V., and Poo, M.M. 1993. Synaptotagmin: a calcium-sensitive inhibitor of exocytosis? Cell, 73: 1247-1249.
26. Rodríguez Del Castillo, A., Lemaire, S., Tchakarov, L., Jeyapragasan, M., Doucet, J.-P., Vitale, M.L., and Trifaró, J.-M. 1990. Chromaffin cell scinderin: a novel calcium-dependent actin filament severing protein. EMBO J. 19: 43-52.
27. 2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5-bisphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation. J. Cell Biol. 119: 797-810.
28. Südhof, T.C., and Jahn, R. 1991. Proteins of synaptic vesicles involved in exocytosis and membrane recycling. Neuron, 6: 665-677.
29. Tchakarov, L., Vitale, M.L., Jeyapragasan, M., Rodríguez Del Castillo, A., and Trifaró, J.-M. 1990. Expression of scinderin, an actin filament-severing protein, in different tissues. FEBS Lett. 268: 209-212.
30. Tchakarov, L., Zhang, L., Rosé, S.D., Tang, R., and Trifaró, J.-M. 1998. Light and electron microscopic study of changes in the organization of the cortical actin cytoskeleton during chromaffin cell secretion. J. Histochem. Cytochem. 46: 193-203.
31. Trifaró, J.-M. 1977. Common mechanisms of hormone secretion. Annu. Rev. Pharmacol. Toxicol. 17: 27-47.
32. Trifaró, J.-M. 1982. The cultured chromaffin cell: a model for the study of biology and pharmacology of paraneurons. Trends Pharmacol. Sci. 3: 389-392.
33. Trifaró, J.-M. 1984. The adrenal paraneuron, its biology and pharmacology. Can. J. Physiol. Pharmacol. 62: 465-466.
34. Trifaró, J.-M. 1990. The 1989 Upjohn Award Lecture: cellular and molecular mechanisms in hormone and neurotransmitter secretion. Can. J. Physiol. Pharmacol. 68: 1-16.
35. Trifaró, J.-M., and Poisner, A.M. 1982. Common properties in the mechanisms of synthesis, processing and storage of secretory products. In The secretory process. Edited by A.M. Poisner and J.-M. Trifaró. Vol. I. The secretory granule. Elsevier/North Holland, New York. pp. 387-407.
36. Trifaró, J.-M., and Vitale, M.L. 1993. Cytoskeleton dynamics during neurotransmitter release. Trends Neurosci. 16: 466-472.
37. Trifaró, J.-M., Bader, M-F., and Doucet, J.P. 1985. Chromaffin cell cytoskeleton: its possible role in secretion. Can. J. Biochem. Cell. Biol. 63: 661-679.
38. Trifaró, J.-M., Novas, M.L., Fournier, S., and Rodríguez Del Castillo, A. 1989. Cellular and molecular mechanisms in hormone and neurotransmitter secretion. In Recent advances in pharmacology and therapeutics. Edited by M. Velasco, A. Israel, E. Romero, and H. Silva. Elsevier Science Publishers, New York. pp. 15-20.
39. Trifaró, J.-M., Vitale, M.L., and Rodríguez Del Castillo, A. 1992. Cytoskeleton and molecular mechanisms in neurotransmitter release by neurosecretory cells. Eur. J. Pharmacol. 225: 83-104.
40. Vitale, M.L., Rodríguez Del Castillo, A., Tchakarov, L., and Trifaró, J.-M. 1991. Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin. J. Cell Biol. 113: 1057-1067.
41. Vitale, M.L., Rodríguez Del Castillo, A., and Trifaró, J.-M. 1992. Protein kinase C activation by phorbol esters induces chromaffin cell cortical filamentous actin disassembly and increases the initial rate of exocytosis in response to nicotinic receptor stimulation. Neuroscience, 51: 463-474.
42. Vitale, M.L., Seward, E.P., and Trifaró, J.-M. 1995. Chromaffin cell cortical actin network dynamics control the size of the release-ready vesicle pool and the initial rate of exocytosis. Neuron, 14: 353-363.
43. 2. Neuron, 17: 287-296.