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PMID: 8552632 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 1 ·1996-01-09 ·Pages 331-5

David C, McPherson PS, Mundigl O, de Camilli P

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.

MeSH Terms
Adaptor Protein Complex 2 Adaptor Protein Complex alpha Subunits Adaptor Proteins, Vesicular Transport Animals Dynamins Endocytosis Fluorescent Antibody Technique, Indirect GTP Phosphohydrolases/metabolism Membrane Proteins/metabolism Nerve Tissue Proteins/physiology Precipitin Tests Protein Binding Rats Synapsins/metabolism Synaptic Vesicles/physiology src Homology Domains
Chemicals
Adaptor Protein Complex 2 Adaptor Protein Complex alpha Subunits Adaptor Proteins, Vesicular Transport Membrane Proteins Nerve Tissue Proteins Synapsins adaptor protein complex 2, alpha 2 subunit amphiphysin GTP Phosphohydrolases Dynamins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
David C
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA.
McPherson P S
Mundigl O
de Camilli P
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.1.331
Published
1996-01-09
Pages
331-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC40232
Subset
IM
Grants
NCI NIH HHS · CA46128 · United States
External Links
PubMed source DOI: 10.1073/pnas.93.1.331 PMC Full Text View journal details
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