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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
44
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pubmed:dateCreated |
2001-10-29
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pubmed:databankReference |
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pubmed:abstractText |
The synaptosome-associated protein of 25 kDa (SNAP-25) interacts with syntaxin 1 and vesicle-associated membrane protein 2 (VAMP2) to form a ternary soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex that is essential for synaptic vesicle exocytosis. We report a novel RING finger protein, Spring, that specifically interacts with SNAP-25. Spring is exclusively expressed in brain and is concentrated at synapses. The association of Spring with SNAP-25 abolishes the ability of SNAP-25 to interact with syntaxin 1 and VAMP2 and prevents the assembly of the SNARE complex. Overexpression of Spring or its SNAP-25-interacting domain reduces Ca(2+)-dependent exocytosis from PC12 cells. These results indicate that Spring may act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP-25 for the SNARE complex formation.
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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/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Snap25 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Stx1a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptosomal-Associated Protein 25,
http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
40824-33
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11524423-Amino Acid Sequence,
pubmed-meshheading:11524423-Animals,
pubmed-meshheading:11524423-Antigens, Surface,
pubmed-meshheading:11524423-Binding, Competitive,
pubmed-meshheading:11524423-Brain,
pubmed-meshheading:11524423-CHO Cells,
pubmed-meshheading:11524423-Calcium,
pubmed-meshheading:11524423-Carrier Proteins,
pubmed-meshheading:11524423-Cricetinae,
pubmed-meshheading:11524423-DNA, Complementary,
pubmed-meshheading:11524423-Exocytosis,
pubmed-meshheading:11524423-Membrane Proteins,
pubmed-meshheading:11524423-Molecular Sequence Data,
pubmed-meshheading:11524423-Nerve Tissue Proteins,
pubmed-meshheading:11524423-PC12 Cells,
pubmed-meshheading:11524423-R-SNARE Proteins,
pubmed-meshheading:11524423-RNA, Messenger,
pubmed-meshheading:11524423-Rats,
pubmed-meshheading:11524423-Sequence Homology, Amino Acid,
pubmed-meshheading:11524423-Synaptic Vesicles,
pubmed-meshheading:11524423-Synaptosomal-Associated Protein 25,
pubmed-meshheading:11524423-Syntaxin 1,
pubmed-meshheading:11524423-Two-Hybrid System Techniques
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pubmed:year |
2001
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pubmed:articleTitle |
Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis.
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pubmed:affiliation |
Department of Pharmacology and Cell and Molecular Physiology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, 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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