Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry

doi:10.1083/jcb.110.1.13

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Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry

T Nakata, K Sobue and N Hirokawa
Department of Anatomy and Cell Biology, School of Medicine, University of Tokyo, Japan.

Calpactin I complex, a calcium-dependent phospholipid-binding protein, promotes aggregation of chromaffin vesicles at physiological micromolar calcium ion levels. Calpactin I complex was found to be a globular molecule with a diameter of 10.7 +/- 1.7 (SD) nm on mica. When liposomes were aggregated by calpactin, quick-freeze, deep-etching revealed fine thin strands (6.5 +/- 1.9 [SD] nm long) cross-linking opposing membranes in addition to the globules on the surface of liposomes. Similar fine strands were also observed between aggregated chromaffin vesicles when they were mixed with calpactin in the presence of Ca2+ ion. In cultured chromaffin cells, similar cross-linking short strands (6-10 nm) were found between chromaffin vesicles and the plasma membrane after stimulation with acetylcholine. Plasma membranes also revealed numerous globular structures approximately 10 nm in diameter on their cytoplasmic surface. Immunoelectron microscopy on frozen ultrathin sections showed that calpactin I was closely associated with the inner face of the plasma membranes and was especially conspicuous between plasma membranes and adjacent vesicles in chromaffin cells. These in vivo and in vitro data strongly suggest that calpactin I complex changes its conformation to cross-link vesicles and the plasma membrane after stimulation of cultured chromaffin cells.
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Beaton, A. R., Rodriguez, J., Reddy, Y. K., Roy, P. (2002). The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release. Proc. Natl. Acad. Sci. USA 99: 13154-13159 [Abstract] [Full Text]
Gerke, V., Moss, S. E. (2002). Annexins: From Structure to Function. Physiol. Rev. 82: 331-371 [Abstract] [Full Text]
Konig, J., Prenen, J., Nilius, B., Gerke, V. (1998). The Annexin II-p11 Complex Is Involved in Regulated Exocytosis in Bovine Pulmonary Artery Endothelial Cells. J. Biol. Chem. 273: 19679-19684 [Abstract] [Full Text]
Caumont, A.-S., Galas, M.-C., Vitale, N., Aunis, D., Bader, M.-F. (1998). Regulated Exocytosis in Chromaffin Cells. TRANSLOCATION OF ARF6 STIMULATES A PLASMA MEMBRANE-ASSOCIATED PHOSPHOLIPASE D. J. Biol. Chem. 273: 1373-1379 [Abstract] [Full Text]
Bellagamba, C., Hubaishy, I., Bjorge, J. D., Fitzpatrick, S. L., Fujita, D. J., Waisman, D. M. (1997). Tyrosine Phosphorylation of Annexin II Tetramer Is Stimulated by Membrane Binding. J. Biol. Chem. 272: 3195-3199 [Abstract] [Full Text]
Diakonova, M, Gerke, V, Ernst, J, Liautard, J., van der Vusse, G, Griffiths, G (1997). Localization of five annexins in J774 macrophages and on isolated phagosomes. J. Cell Sci. 110: 1199-1213 [Abstract]
Jost, M, Zeuschner, D, Seemann, J, Weber, K, Gerke, V (1997). Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes. J. Cell Sci. 110: 221-228 [Abstract]
Biener, Y., Feinstein, R., Mayak, M., Kaburagi, Y., Kadowaki, T., Zick, Y. (1996). Annexin II Is a Novel Player in Insulin Signal Transduction. POSSIBLE ASSOCIATION BETWEEN ANNEXIN II PHOSPHORYLATION AND INSULIN RECEPTOR INTERNALIZATION. J. Biol. Chem. 271: 29489-29496 [Abstract] [Full Text]
Regnouf, F.�o., Sagot, I., Delouche, B., Devilliers, G., Cartaud, J., Henry, J.-P., Pradel, L.-A. (1995). ``In Vitro'' Phosphorylation of Annexin 2 Heterotetramer by Protein Kinase C. J. Biol. Chem. 270: 27143-27150 [Abstract] [Full Text]
Ohnishi, M, Tokuda, M, Masaki, T, Fujimura, T, Tai, Y, Matsui, H, Itano, T, Ishida, T, Takahara, J, Konishi, R, et, al. (1994). Changes in annexin I and II levels during the postnatal development of rat pancreatic islets. J. Cell Sci. 107: 2117-2125 [Abstract]
Lee, T., Lin, Y., Mochitate, K, Grinnell, F (1993). Stress-relaxation of fibroblasts in collagen matrices triggers ectocytosis of plasma membrane vesicles containing actin, annexins II and VI, and beta 1 integrin receptors. J. Cell Sci. 105: 167-177 [Abstract]
Timmons, P., Chan, C., Rigby, P., Poirier, F (1993). The gene encoding the calcium binding protein calcyclin is expressed at sites of exocytosis in the mouse. J. Cell Sci. 104: 187-196 [Abstract]
Creutz, C. (1992). The annexins and exocytosis. Science 258: 924-931 [Abstract]
Thiel, C., Osborn, M., Gerke, V. (1992). The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites. J. Cell Sci. 103: 733-742 [Abstract]