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Cited by 481

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

Shupliakov, Oleg, Löw, Peter, Grabs, Detlev, Gad, Helge, Chen, Hong, David, Carol, Takei, Kohji, De Camilli, Pietro, Brodin, Lennart·1997·Science

Abstract

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.

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Metadata

Authors
Shupliakov, O., Löw, P., Grabs, D., Gad, H., Chen, H., David, C., Takei, K., De Camilli, P., & Brodin, L.
Venue
Science
Published
1997-04-11
Volume
276
Issue
5310
Pages
259-263
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2076364749
Cited by
481
References
0
FWCI
16.68
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions. https://app.cochat.ai/papers/10.1126/science.276.5310.259
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Shupliakov, O., Löw, P., Grabs, D., Gad, H., Chen, H., David, C., Takei, K., De Camilli, P., & Brodin, L. (1997). Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions. Science. https://doi.org/10.1126/science.276.5310.259

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