| pubmed-article:9280305 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9280305 | lifeskim:mentions | umls-concept:C0058836 | lld:lifeskim |
| pubmed-article:9280305 | lifeskim:mentions | umls-concept:C0008905 | lld:lifeskim |
| pubmed-article:9280305 | lifeskim:mentions | umls-concept:C0012727 | lld:lifeskim |
| pubmed-article:9280305 | lifeskim:mentions | umls-concept:C0170270 | lld:lifeskim |
| pubmed-article:9280305 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9280305 | pubmed:dateCreated | 1997-9-23 | lld:pubmed |
| pubmed-article:9280305 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9280305 | pubmed:abstractText | 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. | lld:pubmed |
| pubmed-article:9280305 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9280305 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9280305 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9280305 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9280305 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:9280305 | pubmed:author | pubmed-author:SmithCC | lld:pubmed |
| pubmed-article:9280305 | pubmed:author | pubmed-author:McMahonH THT | lld:pubmed |
| pubmed-article:9280305 | pubmed:author | pubmed-author:WiggePP | lld:pubmed |
| pubmed-article:9280305 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9280305 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:9280305 | pubmed:volume | 413 | lld:pubmed |
| pubmed-article:9280305 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9280305 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9280305 | pubmed:pagination | 319-22 | lld:pubmed |
| pubmed-article:9280305 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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| pubmed-article:9280305 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9280305 | pubmed:articleTitle | Clathrin interacts specifically with amphiphysin and is displaced by dynamin. | lld:pubmed |
| pubmed-article:9280305 | pubmed:affiliation | Neurobiology Division, MRC-LMB, Cambridge, UK. hmm@mrc-lmb.cam.ac.uk | lld:pubmed |
| pubmed-article:9280305 | pubmed:publicationType | Journal Article | lld:pubmed |
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