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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Protein Complex 2
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Adaptor Protein Complex alpha Subunits
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Adaptor Proteins, Vesicular Transport
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Animals
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Dynamins
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Endocytosis
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Fluorescent Antibody Technique, Indirect
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GTP Phosphohydrolases / metabolism*
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Membrane Proteins / metabolism
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Nerve Tissue Proteins / physiology*
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Precipitin Tests
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Protein Binding
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Rats
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Synapsins / metabolism
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Synaptic Vesicles / physiology*
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src Homology Domains
Substances
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Adaptor Protein Complex 2
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Adaptor Protein Complex alpha Subunits
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Adaptor Proteins, Vesicular Transport
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Membrane Proteins
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Nerve Tissue Proteins
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Synapsins
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adaptor protein complex 2, alpha 2 subunit
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amphiphysin
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GTP Phosphohydrolases
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Dynamins