JOURNAL OF CELL BIOLOGY 128(4): 637-645.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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WALCHSOLIMENA, C; BLASI, J; EDELMANN, L; CHAPMAN, ER; Fischer von Mollard, GabrieleUniBi ; JAHN, R
Abstract / Bemerkung
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 similar to 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.
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NSF and SNAP are present on adrenal chromaffin granules.
Burgoyne RD, Williams G., FEBS Lett 414(2), 1997
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Intracellular location of SNAP-25 in human neutrophils.
Nabokina S, Egea G, Blasi J, Mollinedo F., Biochem Biophys Res Commun 239(2), 1997
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Association of the fusion protein NSF with clathrin-coated vesicle membranes.
Steel GJ, Tagaya M, Woodman PG., EMBO J 15(4), 1996
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Distribution of components of the SNARE complex in relation to transmitter release sites at the frog neuromuscular junction.
Boudier JA, Charvin N, Boudier JL, Fathallah M, Tagaya M, Takahashi M, Seagar MJ., Eur J Neurosci 8(3), 1996
PMID: 8963446
Evidence that syntaxin 1A is involved in storage in the secretory pathway.
Bittner MA, Bennett MK, Holz RW., J Biol Chem 271(19), 1996
PMID: 8626670
Growth cone collapse and inhibition of neurite growth by Botulinum neurotoxin C1: a t-SNARE is involved in axonal growth.
Igarashi M, Kozaki S, Terakawa S, Kawano S, Ide C, Komiya Y., J Cell Biol 134(1), 1996
PMID: 8698815
Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport.
Volchuk A, Wang Q, Ewart HS, Liu Z, He L, Bennett MK, Klip A., Mol Biol Cell 7(7), 1996
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Rat and gerbil pinealocytes contain the synaptosomal-associated protein 25 (SNAP-25).
Redecker P, Weyer C, Grube D., J Pineal Res 21(1), 1996
PMID: 8836961
SNAP-25 is present on chromaffin granules and acts as a SNAP receptor.
Tagaya M, Genma T, Yamamoto A, Kozaki S, Mizushima S., FEBS Lett 394(1), 1996
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Differential localization of syntaxin isoforms in polarized Madin-Darby canine kidney cells.
Low SH, Chapin SJ, Weimbs T, Kömüves LG, Bennett MK, Mostov KE., Mol Biol Cell 7(12), 1996
PMID: 8970161
Distinct cellular locations of the syntaxin family of proteins in rat pancreatic acinar cells.
Gaisano HY, Ghai M, Malkus PN, Sheu L, Bouquillon A, Bennett MK, Trimble WS., Mol Biol Cell 7(12), 1996
PMID: 8970162
Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein.
Timmers KI, Clark AE, Omatsu-Kanbe M, Whiteheart SW, Bennett MK, Holman GD, Cushman SW., Biochem J 320 ( Pt 2)(), 1996
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Vesicle-associated proteins and calcium in nerve terminals of chick ciliary ganglia during development of facilitation.
Lin YQ, Brain KL, Nichol KA, Morgan JJ, Bennett MR., J Physiol 497 ( Pt 3)(), 1996
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Molecular mechanisms of protein-mediated membrane fusion.
Hughson FM., Curr Opin Struct Biol 5(4), 1995
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Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis.
Chamberlain LH, Roth D, Morgan A, Burgoyne RD., J Cell Biol 130(5), 1995
PMID: 7657692
Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific vesicle coat protein.
Newman LS, McKeever MO, Okano HJ, Darnell RB., Cell 82(5), 1995
PMID: 7671305
The neuronal exocytotic fusion machine: some new developments.
Chapman ER, Hanson PI, Jahn R., Neuropharmacology 34(11), 1995
PMID: 8606783
Development of cell polarity in budding yeast.
Govindan B, Novick P., J Exp Zool 273(5), 1995
PMID: 8576696

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