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http://hdl.handle.net/2445/25209
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DC Field | Value | Language |
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dc.contributor.author | Walch-Solimena, Christiane | cat |
dc.contributor.author | Blasi Cabús, Joan | cat |
dc.contributor.author | Edelmann, Lambert | cat |
dc.contributor.author | Chapmann, Edwin R. | cat |
dc.contributor.author | Fischer von Mollard, Gabriele | cat |
dc.contributor.author | Jahn, Reinhard | cat |
dc.date.accessioned | 2012-05-09T09:42:45Z | - |
dc.date.available | 2012-05-09T09:42:45Z | - |
dc.date.issued | 1995-02-15 | - |
dc.identifier.issn | 0021-9525 | - |
dc.identifier.uri | http://hdl.handle.net/2445/25209 | - |
dc.description.abstract | Syntaxin 1 and synaptosome-associated protein of 25 kD (SNAP-25) are neuronal plasmalemma proteins that appear to be essential for exocytosis of synaptic vesicles (SVs). Both proteins form a complex with synaptobrevin, an intrinsic membrane protein of SVs. This binding is thought to be responsible for vesicle docking and apparently precedes membrane fusion. According to the current concept, syntaxin 1 and SNAP-25 are members of larger protein families, collectively designated as target-SNAP receptors (t-SNAREs), whose specific localization to subcellular membranes define where transport vesicles bind and fuse. Here we demonstrate that major pools of syntaxin 1 and SNAP-25 recycle with SVs. Both proteins cofractionate with SVs and clathrin-coated vesicles upon subcellular fractionation. Using recombinant proteins as standards for quantitation, we found that syntaxin 1 and SNAP-25 each comprise approximately 3% of the total protein in highly purified SVs. Thus, both proteins are significant components of SVs although less abundant than synaptobrevin (8.7% of the total protein). Immunoisolation of vesicles using synaptophysin and syntaxin specific antibodies revealed that most SVs contain syntaxin 1. The widespread distribution of both syntaxin 1 and SNAP-25 on SVs was further confirmed by immunogold electron microscopy. Botulinum neurotoxin C1, a toxin that blocks exocytosis by proteolyzing syntaxin 1, preferentially cleaves vesicular syntaxin 1. We conclude that t-SNAREs participate in SV recycling in what may be functionally distinct forms. | eng |
dc.format.extent | 9 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | eng |
dc.publisher | Rockefeller University Press | - |
dc.relation.isformatof | Reproducció digital del document publicat a: http://dx.doi.org/10.1083/jcb.128.4.637 | - |
dc.relation.ispartof | Journal of Cell Biology, 1995, vol. 128, núm. 4, p. 637-645 | - |
dc.relation.uri | http://dx.doi.org/10.1083/jcb.128.4.637 | - |
dc.rights | (c) Rockefeller University Press, 1995 | - |
dc.source | Articles publicats en revistes (Patologia i Terapèutica Experimental) | - |
dc.subject.classification | Neurones | cat |
dc.subject.classification | Sinapsi | cat |
dc.subject.classification | Neurotransmissió | cat |
dc.subject.classification | Interacció cel·lular | cat |
dc.subject.other | Neurons | eng |
dc.subject.other | Synapses | eng |
dc.subject.other | Neural transmission | eng |
dc.subject.other | Cell interaction | eng |
dc.title | The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling | eng |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 92437 | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 7860636 | - |
Appears in Collections: | Articles publicats en revistes (Patologia i Terapèutica Experimental) |
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