A small GTP-binding protein dissociates from synaptic vesicles during exocytosis (original) (raw)
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- Published: 03 January 1991
Nature volume 349, pages 79–81 (1991)Cite this article
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Abstract
LOW-molecular-weight GTP-binding proteins are strong candidates for regulators of membrane traffic1–3. In yeast, mutations in the sec4 or ypt1 genes encoding small GTP-binding proteins inhibit constitutive membrane flow at the plasma membrane or Golgi complex, respectively4–6. It has been suggested that membrane fusion–fission events are regulated by cycling of small GTP-binding proteins between a membrane-bound and free state7, but although most of these small proteins are found in both soluble and tightly membrane-bound forms, there is no direct evidence to support such cycling. In rat brain a small GTP-binding protein, rab3 A, is exclusively associated with synaptic vesicles, the secretory organelles of nerve terminals8,9. Here we use isolated nerve terminals to study the fate of rab3A during synaptic vesicle exocytosis. We find that rab3A dissociates quantitatively from the vesicle membrane after Ca2+-dependent exocytosis and that this dissociation is partially reversible during recovery after stimulation. These results are direct evidence for an association–dissociation cycle of a small GTP-binding protein during traffic of its host membrane.
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Author notes
- Reinhard Jahn: To whom correspondence should be addressed.
Authors and Affiliations
- Department of Neurochemistry, Max-Planck Institute for Psychiatry, Am Klopferspitz 18a, D-8033, Martinsried, Germany
Gabriele Fischer von Mollard & Reinhard Jahn - Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas, 75235, USA
Thomas C. Südhof
Authors
- Gabriele Fischer von Mollard
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von Mollard, G., Südhof, T. & Jahn, R. A small GTP-binding protein dissociates from synaptic vesicles during exocytosis.Nature 349, 79–81 (1991). https://doi.org/10.1038/349079a0
- Received: 30 August 1990
- Accepted: 22 October 1990
- Issue Date: 03 January 1991
- DOI: https://doi.org/10.1038/349079a0