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Science 11 April 1997:
Vol. 276. no. 5310, pp. 259 - 263
DOI: 10.1126/science.276.5310.259
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Reports

Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions

Oleg Shupliakov, Peter Löw, Detlev Grabs, * Helge Gad, Hong Chen, Carol David, dagger Kohji Takei, Pietro De Camilli, ddagger Lennart Brodin ddagger

The proline-rich COOH-terminal region of dynamin binds various Src homology 3 (SH3) domain-containing proteins, but the physiological role of these interactions is unknown. In living nerve terminals, the function of the interaction with SH3 domains was examined. Amphiphysin contains an SH3 domain and is a major dynamin binding partner at the synapse. Microinjection of amphiphysin's SH3 domain or of a dynamin peptide containing the SH3 binding site inhibited synaptic vesicle endocytosis at the stage of invaginated clathrin-coated pits, which resulted in an activity-dependent distortion of the synaptic architecture and a depression of transmitter release. These findings demonstrate that SH3-mediated interactions are required for dynamin function and support an essential role of clathrin-mediated endocytosis in synaptic vesicle recycling.

O. Shupliakov, P. Löw, H. Gad, L. Brodin, The Nobel Institute for Neurophysiology, Department of Neuroscience, Karolinska Institutet, S-171 77 Stockholm, Sweden.
D. Grabs, H. Chen, C. David, K. Takei, P. De Camilli, Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.
*   Present address: Institut für Anatomie/Charité, Philippstrasse 12, D-10115 Berlin, Germany.

dagger    Present address: Department of Immunology, Weizmann Institute of Science, 76100 Rehovot, Israel.

ddagger    To whom correspondence should be addressed. E-mail: pietro_decamilli{at}quickmail.yale.edu (for P. De Camilli); lennart.brodin{at}neuro.ki.se (for L. Brodin)

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A Complex Web of Signal-dependent Trafficking Underlies the Triorganellar Distribution of P-Selectin in Neuroendocrine PC12 Cells.
A. D. Blagoveshchenskaya, E. W. Hewitt, and D. F. Cutler (1999)
J. Cell Biol. 145, 1419-1433
   Abstract »    Full Text »    PDF »
EHSH1/Intersectin, a Protein That Contains EH and SH3 Domains and Binds to Dynamin and SNAP-25. A PROTEIN CONNECTION BETWEEN EXOCYTOSIS AND ENDOCYTOSIS?.
M. Okamoto, S. Schoch, and T. C. Sudhof (1999)
J. Biol. Chem. 274, 18446-18454
   Abstract »    Full Text »    PDF »
Coupled Inositide Phosphorylation and Phospholipase D Activation Initiates Clathrin-coat Assembly on Lysosomes.
L. S. Arneson, J. Kunz, R. A. Anderson, and L. M. Traub (1999)
J. Biol. Chem. 274, 17794-17805
   Abstract »    Full Text »    PDF »
Splice Variants of Intersectin Are Components of the Endocytic Machinery in Neurons and Nonneuronal Cells.
N. K. Hussain, M. Yamabhai, A. R. Ramjaun, A. M. Guy, D. Baranes, J. P. O'Bryan, C. J. Der, B. K. Kay, and P. S. McPherson (1999)
J. Biol. Chem. 274, 15671-15677
   Abstract »    Full Text »    PDF »
Calcium Channels Involved in Synaptic Transmission From Reticulospinal Axons in Lamprey.
P. Krieger, A. Buschges, and A. el Manira (1999)
J Neurophysiol 81, 1699-1705
   Abstract »    Full Text »    PDF »
Syndapin I, a Synaptic Dynamin-binding Protein that Associates with the Neural Wiskott-Aldrich Syndrome Protein.
B. Qualmann, J. Roos, P. J. DiGregorio, and R. B. Kelly (1999)
Mol. Biol. Cell 10, 501-513
   Abstract »    Full Text »
Involvement of Long Chain Fatty Acid Elongation in the Trafficking of Secretory Vesicles in Yeast.
D. David, S. Sundarababu, and J. E. Gerst (1998)
J. Cell Biol. 143, 1167-1182
   Abstract »    Full Text »    PDF »
Paralemmin, a Prenyl-Palmitoyl-anchored Phosphoprotein Abundant in Neurons and Implicated in Plasma Membrane Dynamics and Cell Process Formation.
C. Kutzleb, G. Sanders, R. Yamamoto, X. Wang, B. Lichte, E. Petrasch-Parwez, and M. W. Kilimann (1998)
J. Cell Biol. 143, 795-813
   Abstract »    Full Text »    PDF »
The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding.
D. E. Klein, A. Lee, D. W. Frank, M. S. Marks, and M. A. Lemmon (1998)
J. Biol. Chem. 273, 27725-27733
   Abstract »    Full Text »    PDF »


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