| pubmed-article:10704453 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10704453 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
| pubmed-article:10704453 | lifeskim:mentions | umls-concept:C0597361 | lld:lifeskim |
| pubmed-article:10704453 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
| pubmed-article:10704453 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:10704453 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10704453 | pubmed:dateCreated | 2000-4-25 | lld:pubmed |
| pubmed-article:10704453 | pubmed:abstractText | Syndapin I (SdpI) interacts with proteins involved in endocytosis and actin dynamics and was therefore proposed to be a molecular link between the machineries for synaptic vesicle recycling and cytoskeletal organization. We here report the identification and characterization of SdpII, a ubiquitously expressed isoform of the brain-specific SdpI. Certain splice variants of rat SdpII in other species were named FAP52 and PACSIN 2. SdpII binds dynamin I, synaptojanin, synapsin I, and the neural Wiskott-Aldrich syndrome protein (N-WASP), a stimulator of Arp2/3 induced actin filament nucleation. In neuroendocrine cells, SdpII colocalizes with dynamin, consistent with a role for syndapin in dynamin-mediated endocytic processes. The src homology 3 (SH3) domain of SdpI and -II inhibited receptor-mediated internalization of transferrin, demonstrating syndapin involvement in endocytosis in vivo. Overexpression of full-length syndapins, but not the NH(2)-terminal part or the SH3 domains alone, had a strong effect on cortical actin organization and induced filopodia. This syndapin overexpression phenotype appears to be mediated by the Arp2/3 complex at the cell periphery because it was completely suppressed by coexpression of a cytosolic COOH-terminal fragment of N-WASP. Consistent with a role in actin dynamics, syndapins localized to sites of high actin turnover, such as filopodia tips and lamellipodia. Our results strongly suggest that syndapins link endocytosis and actin dynamics. | lld:pubmed |
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| pubmed-article:10704453 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10704453 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10704453 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10704453 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10704453 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10704453 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10704453 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:10704453 | pubmed:author | pubmed-author:KellyR BRB | lld:pubmed |
| pubmed-article:10704453 | pubmed:author | pubmed-author:QualmannBB | lld:pubmed |
| pubmed-article:10704453 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10704453 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:10704453 | pubmed:volume | 148 | lld:pubmed |
| pubmed-article:10704453 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10704453 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10704453 | pubmed:pagination | 1047-62 | lld:pubmed |
| pubmed-article:10704453 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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