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Sci. STKE, 21 December 2004
Vol. 2004, Issue 264, p. re19
[DOI: 10.1126/stke.2642004re19]

REVIEWS

Cycling of Synaptic Vesicles: How Far? How Fast!

Thierry Galli1* and Volker Haucke2*

1Membrane Traffic and Neuronal Plasticity Group, INSERM U536, Institut du Fer-à-moulin, 75005 Paris, France.
2Institut für Chemie-Biochemie, Freie Universität Berlin, D-14195 Berlin, Germany.

Gloss: Synaptic vesicles are the major secretory organelles within the nervous system that store and secrete nonpeptide neurotransmitters. Upon electrical stimulation and the consequent influx of calcium into the presynaptic nerve terminal, a fraction of the synaptic vesicles fuses with the plasma membrane and releases its neurotransmitter content into the synaptic cleft. Because the nerve terminal can be far away from the protein synthesis machinery, which is located in the somatodendritic part of a neuron, synaptic vesicles are regenerated locally by recycling. Physiological experiments indicate that in addition to the well-established slow mode for the cycling of vesicles, many synapses may have the capacity to regenerate fusion-competent synaptic vesicles by a much faster pathway within seconds. Although the same fusion machinery appears to be utilized by both the fast and slow tracks of vesicle cycling, a number of unique components are involved in the slow reformation of synaptic vesicles by clathrin-mediated endocytosis. In this STKE Review, which includes 2 figures, 2 animations, and 217 citations, we describe here the unique and the shared components of each track and attempt to identify common mechanisms that could serve as a link between these pathways.

*Corresponding authors. E-mail, thierry{at}tgalli.net (T.G.) or vhaucke{at}chemie.fu-berlin.de (V.H.)

Citation: T. Galli, V. Haucke, Cycling of Synaptic Vesicles: How Far? How Fast! Sci. STKE 2004, re19 (2004).


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Compromised fidelity of endocytic synaptic vesicle protein sorting in the absence of stonin 2.
N. L. Kononenko, M. K. Diril, D. Puchkov, M. Kintscher, S. J. Koo, G. Pfuhl, Y. Winter, M. Wienisch, J. Klingauf, J. Breustedt, et al. (2013)
PNAS 110, E526-E535
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Role of TI-VAMP and CD82 in EGFR cell-surface dynamics and signaling.
L. Danglot, M. Chaineau, M. Dahan, M.-C. Gendron, N. Boggetto, F. Perez, and T. Galli (2010)
J. Cell Sci. 123, 723-735
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Molecular Basis for Association of PIPKI{gamma}-p90 with Clathrin Adaptor AP-2.
N. Kahlfeldt, A. Vahedi-Faridi, S. J. Koo, J. G. Schafer, G. Krainer, S. Keller, W. Saenger, M. Krauss, and V. Haucke (2010)
J. Biol. Chem. 285, 2734-2749
   Abstract »    Full Text »    PDF »
Role of HRB in Clathrin-dependent Endocytosis.
M. Chaineau, L. Danglot, V. Proux-Gillardeaux, and T. Galli (2008)
J. Biol. Chem. 283, 34365-34373
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Molecular basis of synaptic vesicle cargo recognition by the endocytic sorting adaptor stonin 2.
N. Jung, M. Wienisch, M. Gu, J. B. Rand, S. L. Muller, G. Krause, E. M. Jorgensen, J. Klingauf, and V. Haucke (2007)
J. Cell Biol. 179, 1497-1510
   Abstract »    Full Text »    PDF »
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.
M. Masuda, S. Takeda, M. Sone, T. Ohki, H. Mori, Y. Kamioka, and N. Mochizuki (2006)
EMBO J. 25, 2889-2897
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