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| Subject Categories:
Signal Transduction
| Neuroscience
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The EMBO Journal
(2005) 24, 2114–2126, doi:10.1038/sj.emboj.7600696 Published online 26 May 2005
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| v-SNAREs control exocytosis of vesicles from priming to fusion |
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Maria Borisovska1, Ying Zhao1, Yaroslav Tsytsyura1, Nataliya Glyvuk1, Shigeo Takamori2, Ulf Matti1, Jens Rettig1, Thomas Südhof3 and Dieter Bruns1
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1 Department of Physiology, University of Saarland, Homburg/Saar, Germany
2 Department of Neurobiology, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany
3 Center for Basic Neuroscience, Howard Hughes Medical Institute, University of Texas Southwestern, Dallas, TX, USA
To whom correspondence should be addressed
Dieter Bruns, Department of Physiology, University of Saarland, Kirrbergerstrasse 8, 66424 Homburg/Saar, Germany. Tel.: +49 6841 162 6495; Fax: +49 6841 162 6492; E-mail: dieter.bruns@uniklinik-saarland.de
Received 31 January 2005; Accepted 3 May 2005; Published online 26 May 2005.
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| Abstract |
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| SNARE proteins (soluble NSF-attachment protein receptors) are thought to be central components of the exocytotic mechanism in neurosecretory cells, but their precise function remained unclear. Here, we show that each of the vesicle-associated SNARE proteins (v-SNARE) of a chromaffin granule, synaptobrevin II or cellubrevin, is sufficient to support Ca2+-dependent exocytosis and to establish a pool of primed, readily releasable vesicles. In the absence of both proteins, secretion is abolished, without affecting biogenesis or docking of granules indicating that v-SNAREs are absolutely required for granule exocytosis. We find that synaptobrevin II and cellubrevin differentially control the pool of readily releasable vesicles and show that the v-SNARE's amino terminus regulates the vesicle's primed state. We demonstrate that dynamics of fusion pore dilation are regulated by v-SNAREs, indicating their action throughout exocytosis from priming to fusion of vesicles. |
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| Keywords: amperometry, capacitance measurements, cellubrevin, chromaffin cells, synaptobrevin II |
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