| pubmed-article:14532001 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14532001 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:14532001 | lifeskim:mentions | umls-concept:C1154462 | lld:lifeskim |
| pubmed-article:14532001 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:14532001 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:14532001 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
| pubmed-article:14532001 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:14532001 | pubmed:dateCreated | 2003-10-8 | lld:pubmed |
| pubmed-article:14532001 | pubmed:abstractText | A tight balance between synaptic vesicle exocytosis and endocytosis is fundamental to maintaining synaptic structure and function. Calcium influx through voltage-gated Ca2+ channels is crucial in regulating synaptic vesicle exocytosis. However, much less is known about how Ca2+ regulates vesicle endocytosis or how the endocytic machinery becomes enriched at the nerve terminal. We report here a direct interaction between voltage-gated Ca2+ channels and endophilin, a key regulator of clathrin-mediated synaptic vesicle endocytosis. Formation of the endophlin-Ca2+ channel complex is Ca2+ dependent. The primary Ca2+ binding domain resides within endophilin and regulates both endophilin-Ca2+ channel and endophilin-dynamin complexes. Introduction into hippocampal neurons of a dominant-negative endophilin construct, which constitutively binds to Ca2+ channels, significantly reduces endocytosis-mediated uptake of FM 4-64 dye without abolishing exocytosis. These results suggest an important role for Ca2+ channels in coordinating synaptic vesicle recycling by directly coupling to both exocytotic and endocytic machineries. | lld:pubmed |
| pubmed-article:14532001 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14532001 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14532001 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14532001 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14532001 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:ChenYuanY | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:ChangShaohuaS | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:ChenGongG | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:Maeno-Hikichi... | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:LaiMeizanM | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:ZhangJi-fangJ... | lld:pubmed |
| pubmed-article:14532001 | pubmed:author | pubmed-author:DengLunbinL | lld:pubmed |
| pubmed-article:14532001 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14532001 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:14532001 | pubmed:volume | 115 | lld:pubmed |
| pubmed-article:14532001 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14532001 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14532001 | pubmed:pagination | 37-48 | lld:pubmed |
| pubmed-article:14532001 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:14532001 | pubmed:meshHeading | pubmed-meshheading:14532001... | lld:pubmed |
| pubmed-article:14532001 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14532001 | pubmed:articleTitle | Formation of an endophilin-Ca2+ channel complex is critical for clathrin-mediated synaptic vesicle endocytosis. | lld:pubmed |
| pubmed-article:14532001 | pubmed:affiliation | Department of Pharmacology, University of Pennsylvania School of Medicine, 3620 Hamilton Walk, Philadelphia, PA 19104, USA. | lld:pubmed |
| pubmed-article:14532001 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14532001 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14532001 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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