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Cited by 409

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A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals.

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David, C, McPherson, P S, Mundigl, O, de Camilli, P·1996·Proceedings of the National Academy of Sciences

Abstract

Amphiphysin, a major autoantigen in paraneoplastic Stiff-Man syndrome, is an SH3 domain-containing neuronal protein, concentrated in nerve terminals. Here, we demonstrate a specific, SH3 domain-mediated, interaction between amphiphysin and dynamin by gel overlay and affinity chromatography. In addition, we show that the two proteins are colocalized in nerve terminals and are coprecipitated from brain extracts consistent with their interactions in situ. We also report that a region of amphiphysin distinct from its SH3 domain mediates its binding to the alpha c subunit of AP2 adaptin, which is also concentrated in nerve terminals. These findings support a role of amphiphysin in synaptic vesicle endocytosis.

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Metadata

Authors
David, C., McPherson, P. S., Mundigl, O., & de Camilli, P.
Venue
Proceedings of the National Academy of Sciences
Published
1996-01-09
Volume
93
Issue
1
Pages
331-335
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975081377
Cited by
409
References
0
FWCI
15.15
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. https://app.cochat.ai/papers/10.1073/pnas.93.1.331
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David, C., McPherson, P. S., Mundigl, O., & de Camilli, P. (1996). A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.1.331

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.