| pubmed-article:9950691 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9950691 | lifeskim:mentions | umls-concept:C0258432 | lld:lifeskim |
| pubmed-article:9950691 | lifeskim:mentions | umls-concept:C0599851 | lld:lifeskim |
| pubmed-article:9950691 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:9950691 | lifeskim:mentions | umls-concept:C1418241 | lld:lifeskim |
| pubmed-article:9950691 | lifeskim:mentions | umls-concept:C1428968 | lld:lifeskim |
| pubmed-article:9950691 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9950691 | pubmed:dateCreated | 1999-3-18 | lld:pubmed |
| pubmed-article:9950691 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9950691 | pubmed:abstractText | The GTPase dynamin has been clearly implicated in clathrin-mediated endocytosis of synaptic vesicle membranes at the presynaptic nerve terminal. Here we describe a novel 52-kDa protein in rat brain that binds the proline-rich C terminus of dynamin. Syndapin I (synaptic, dynamin-associated protein I) is highly enriched in brain where it exists in a high molecular weight complex. Syndapin I can be involved in multiple protein-protein interactions via a src homology 3 (SH3) domain at the C terminus and two predicted coiled-coil stretches. Coprecipitation studies and blot overlay analyses revealed that syndapin I binds the brain-specific proteins dynamin I, synaptojanin, and synapsin I via an SH3 domain-specific interaction. Coimmunoprecipitation of dynamin I with antibodies recognizing syndapin I and colocalization of syndapin I with dynamin I at vesicular structures in primary neurons indicate that syndapin I associates with dynamin I in vivo and may play a role in synaptic vesicle endocytosis. Furthermore, syndapin I associates with the neural Wiskott-Aldrich syndrome protein, an actin-depolymerizing protein that regulates cytoskeletal rearrangement. These characteristics of syndapin I suggest a molecular link between cytoskeletal dynamics and synaptic vesicle recycling in the nerve terminal. | lld:pubmed |
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| pubmed-article:9950691 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9950691 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9950691 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9950691 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9950691 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9950691 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9950691 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:9950691 | pubmed:author | pubmed-author:KellyR BRB | lld:pubmed |
| pubmed-article:9950691 | pubmed:author | pubmed-author:RoosJJ | lld:pubmed |
| pubmed-article:9950691 | pubmed:author | pubmed-author:QualmannBB | lld:pubmed |
| pubmed-article:9950691 | pubmed:author | pubmed-author:DiGregorioP... | lld:pubmed |
| pubmed-article:9950691 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9950691 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:9950691 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9950691 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9950691 | pubmed:pagination | 501-13 | lld:pubmed |
| pubmed-article:9950691 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:9950691 | pubmed:meshHeading | pubmed-meshheading:9950691-... | lld:pubmed |
| pubmed-article:9950691 | pubmed:meshHeading | pubmed-meshheading:9950691-... | lld:pubmed |
| pubmed-article:9950691 | pubmed:meshHeading | pubmed-meshheading:9950691-... | lld:pubmed |
