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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-10-8
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SH3GL2 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
115
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37-48
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14532001-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:14532001-Animals,
pubmed-meshheading:14532001-Binding Sites,
pubmed-meshheading:14532001-Calcium,
pubmed-meshheading:14532001-Calcium Channels,
pubmed-meshheading:14532001-Carrier Proteins,
pubmed-meshheading:14532001-Cells, Cultured,
pubmed-meshheading:14532001-Clathrin,
pubmed-meshheading:14532001-Dynamins,
pubmed-meshheading:14532001-Electrophysiology,
pubmed-meshheading:14532001-Endocytosis,
pubmed-meshheading:14532001-Humans,
pubmed-meshheading:14532001-Macromolecular Substances,
pubmed-meshheading:14532001-Neurons,
pubmed-meshheading:14532001-Presynaptic Terminals,
pubmed-meshheading:14532001-Protein Structure, Tertiary,
pubmed-meshheading:14532001-Rats,
pubmed-meshheading:14532001-Rats, Sprague-Dawley,
pubmed-meshheading:14532001-Recombinant Fusion Proteins,
pubmed-meshheading:14532001-Synaptic Transmission,
pubmed-meshheading:14532001-Synaptic Vesicles,
pubmed-meshheading:14532001-Two-Hybrid System Techniques
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pubmed:year |
2003
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pubmed:articleTitle |
Formation of an endophilin-Ca2+ channel complex is critical for clathrin-mediated synaptic vesicle endocytosis.
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pubmed:affiliation |
Department of Pharmacology, University of Pennsylvania School of Medicine, 3620 Hamilton Walk, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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