Clathrin interacts specifically with amphiphysin and is displaced by dynamin 1

Amphiphysin is an SH3 domain protein that has been implicated in synaptic vesicle endocytosis. We have recently cloned a second amphiphysin isoform, Amph2 (sequence submitted to GenBank, Y13380). Proteins capable of forming a complex with amphiphysin were isolated from rat brain by using recombinant...

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Bibliographic Details
Published in:FEBS letters 1997-08, Vol.413 (2), p.319-322
Main Authors: McMahon, Harvey T, Wigge, Patrick, Smith, Corrin
Format: Article
Language:English
Subjects:
adaptor protein complex 2
Amph
Amphiphysin
AP-2
Clathrin
Coated pit
Dynamin
glutathione-S-transferase
GST
GTP
guanosine triphosphate
PAGE
polyacrylamide gel electrophoresis
SH3
src-homology 3
Synaptic vesicle Endocytosis
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Summary:Amphiphysin is an SH3 domain protein that has been implicated in synaptic vesicle endocytosis. We have recently cloned a second amphiphysin isoform, Amph2 (sequence submitted to GenBank, Y13380). Proteins capable of forming a complex with amphiphysin were isolated from rat brain by using recombinant GST‐Amph2 for binding experiments. As well as interacting with dynamin I, the full‐length protein bound to a weaker 180‐kDa band. Immunoblotting demonstrated this protein to be clathrin. To address whether this is a direct interaction, the clathrin binding to amphiphysin was reconstituted in vitro with purified proteins. The N‐terminal domain of Amph2 is sufficient for clathrin binding. Dynamin, which interacts with the SH3 domain of Amph2, displaces clathrin from the N‐terminus. We propose a model that may explain how clathrin and dynamin are recruited to non‐overlapping sites of the coated pit.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00928-9