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Volumn 10, Issue 4, 1998, Pages 483-492

Docking and fusion in neurosecretion

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; N ETHYLMALEIMIDE; NEUROTRANSMITTER;

EID: 0032146628     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80063-X     Document Type: Article
Times cited : (74)

References (74)
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    • Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation
    • of special interest. These two studies [46,47] examine structural changes that occur upon the binding of soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors (SNAREs) to each other. Circular dichroism spectroscopy is used to determine α-helical content of SNAREs. Syntaxin binding induces a large increase in α-helicity in both synaptosome-associated protein of 25 kDa SNAP-25 and synaptobrevin/VAMP. The stoichiometry of SNARE associations change from a 2:1 syntaxin:SNAP-25 complex to a 1:1:1 ternary complex, and the ternary complex is highly thermostable. The authors propose that structural changes help overcome energy barriers for membrane fusion.
    • Fasshauer D, Otto H, Eliason WK, Jahn R, Brunger AT. Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. of special interest J Biol Chem. 272:1997;28036-28041 These two studies [46,47] examine structural changes that occur upon the binding of soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors (SNAREs) to each other. Circular dichroism spectroscopy is used to determine α-helical content of SNAREs. Syntaxin binding induces a large increase in α-helicity in both synaptosome-associated protein of 25 kDa SNAP-25 and synaptobrevin/VAMP. The stoichiometry of SNARE associations change from a 2:1 syntaxin:SNAP-25 complex to a 1:1:1 ternary complex, and the ternary complex is highly thermostable. The authors propose that structural changes help overcome energy barriers for membrane fusion.
    • (1997) J Biol Chem , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3    Jahn, R.4    Brunger, A.T.5
  • 49
    • 0032489507 scopus 로고    scopus 로고
    • Organelle membrane fusion: A novel function for the syntaxin homolog Ufe1p in ER membrane fusion
    • of special interest. Ufe1p, the yeast homolog of syntaxin 5, is required for endoplasmic reticulum membrane fusion, which is mediated by cdc48, the yeast homolog of p97. No apparent involvement of a v-SNARE was detected.
    • Patel SK, Indig FE, Olivieri N, Levine ND, Latterich M. Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion. of special interest Cell. 92:1998;611-620 Ufe1p, the yeast homolog of syntaxin 5, is required for endoplasmic reticulum membrane fusion, which is mediated by cdc48, the yeast homolog of p97. No apparent involvement of a v-SNARE was detected.
    • (1998) Cell , vol.92 , pp. 611-620
    • Patel, S.K.1    Indig, F.E.2    Olivieri, N.3    Levine, N.D.4    Latterich, M.5
  • 50
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    • Syntaxin 5 is a common componenet of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • of special interest. The fusion of vesiculated Golgi membranes requires two ATPases, NSF and p97. This study shows that α-SNAP can inhibit the p97 pathway, whereas p47, a component of the p97 pathway, can inhibit the NSF pathway. The t-SNARE syntaxin 5 appears to be a component common to both pathways.
    • Rabouille C, Kondo H, Newman R, Hui N, Freemont R, Warren G. Syntaxin 5 is a common componenet of the NSF-and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. of special interest Cell. 92:1998;603-610 The fusion of vesiculated Golgi membranes requires two ATPases, NSF and p97. This study shows that α-SNAP can inhibit the p97 pathway, whereas p47, a component of the p97 pathway, can inhibit the NSF pathway. The t-SNARE syntaxin 5 appears to be a component common to both pathways.
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, R.5    Warren, G.6
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    • Laage, R.1    Langosch, D.2
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    • The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
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    • SNAP-25 is present on chromaffin granules and acts as a SNAP receptor
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    • RbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin
    • Garcia EP, McPherson PS, Chilcote TJ, Takei K, De Camilli P. rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin. J Cell Biol. 129:1995;105-120.
    • (1995) J Cell Biol , vol.129 , pp. 105-120
    • Garcia, E.P.1    McPherson, P.S.2    Chilcote, T.J.3    Takei, K.4    De Camilli, P.5
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    • Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles
    • of special interest. SDS-resistant complexes containing syntaxin, SNAP-25, and synaptobrevin/VAMP can form in synaptic vesicle extracts. The addition of NSF and SNAPs to these extracts causes partial disassembly of the complexes. Toxin cleavage experiments show that most of the vesicular syntaxin and SNAP-25 are in a complex with synaptobrevin/VAMP; however, most of the synaptobrevin/VAMP on synaptic vesicles is not complexed with t-SNAREs.
    • Otto H, Hanson PI, Jahn R. Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles. of special interest Proc Natl Acad Sci USA. 94:1997;6197-6201 SDS-resistant complexes containing syntaxin, SNAP-25, and synaptobrevin/VAMP can form in synaptic vesicle extracts. The addition of NSF and SNAPs to these extracts causes partial disassembly of the complexes. Toxin cleavage experiments show that most of the vesicular syntaxin and SNAP-25 are in a complex with synaptobrevin/VAMP; however, most of the synaptobrevin/VAMP on synaptic vesicles is not complexed with t-SNAREs.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6197-6201
    • Otto, H.1    Hanson, P.I.2    Jahn, R.3
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    • Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates
    • of special interest. Syntaxin 5 is found on endoplasmic reticulum derived vesicles in a 20S SNARE complex and is required for transport from the endoplasmic reticulum to the Golgi.
    • Rowe T, Dascher C, Bannykh S, Plutner H, Balch WE. Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates. of special interest Science. 279:1998;696-700 Syntaxin 5 is found on endoplasmic reticulum derived vesicles in a 20S SNARE complex and is required for transport from the endoplasmic reticulum to the Golgi.
    • (1998) Science , vol.279 , pp. 696-700
    • Rowe, T.1    Dascher, C.2    Bannykh, S.3    Plutner, H.4    Balch, W.E.5
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    • A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
    • of outstanding interest. Yeast vacuoles contain v - t-SNARE complexes, and Sec17p, Sec18p, and ATP are required to disassemble these complexes. Sec17p and Sec18p are also required to prime vacuoles that contain only t-SNAREs, but not vacuoles containing only v-SNAREs. This important study confirms a role for NSF in priming t-SNAREs, in addition to its role in disassembly of SNARE complexes.
    • Ungermann C, Nichols BJ, Pelham HRB, Wickner W. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. of outstanding interest J Cell Biol. 140:1998;61-69 Yeast vacuoles contain v - t-SNARE complexes, and Sec17p, Sec18p, and ATP are required to disassemble these complexes. Sec17p and Sec18p are also required to prime vacuoles that contain only t-SNAREs, but not vacuoles containing only v-SNAREs. This important study confirms a role for NSF in priming t-SNAREs, in addition to its role in disassembly of SNARE complexes.
    • (1998) J Cell Biol , vol.140 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.B.3    Wickner, W.4
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    • LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex and is released during fusion
    • Xu Z, Wickner W. LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex and is released during fusion. Cell. 93:1998;1125-1134.
    • (1998) Cell , vol.93 , pp. 1125-1134
    • Xu, Z.1    Wickner, W.2
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    • Synaptic vesicle biogenesis, docking, and fusion: A molecular description
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    • T-SNARE activation through transient interaction with a rab-like guanosine triphosphatase
    • of special interest. Immunoprecipitation analysis of yeast spheroplasts indicates that both the Rab protein Yp11p and the Sec1 protein Sly1p can interact separately with the t-SNARE Sed5p. Since both v - t-SNARE interactions and t-SNARE - Sly1p interactions are sensitive to the amount of Ypt1p present, the authors present a model for regulation of v - t-SNARE complexes, which suggests that Sly1p interacts first with the t-SNARE and is then displaced transiently by Ypt1p to regulate v - t-SNARE complex assembly.
    • Lupashin VV, Waters MG. t-SNARE activation through transient interaction with a rab-like guanosine triphosphatase. of special interest Science. 276:1997;1255-1258 Immunoprecipitation analysis of yeast spheroplasts indicates that both the Rab protein Yp11p and the Sec1 protein Sly1p can interact separately with the t-SNARE Sed5p. Since both v - t-SNARE interactions and t-SNARE - Sly1p interactions are sensitive to the amount of Ypt1p present, the authors present a model for regulation of v - t-SNARE complexes, which suggests that Sly1p interacts first with the t-SNARE and is then displaced transiently by Ypt1p to regulate v - t-SNARE complex assembly.
    • (1997) Science , vol.276 , pp. 1255-1258
    • Lupashin, V.V.1    Waters, M.G.2
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    • N-ethylmaleimide-sensitive factor (NSF) and α-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex
    • Subramaniam VN, Loh E, Hong W. N-ethylmaleimide-sensitive factor (NSF) and α-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex. J Biol Chem. 272:1997;25441-25444.
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    • Subramaniam, V.N.1    Loh, E.2    Hong, W.3
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    • Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis
    • of special interest. A mutation in α-SNAP results in a decreased ability to stimulate NSF ATPase activity. The mutant protein does not disassemble 20S SNARE complexes, but binds to NSF normally. In addition, this mutant does not stimulate exocytosis in permeabilized chromaffi cells, unlike wild-type α-SNAP. This study therefore emphasizes the role of α-SNAP in stimulating the ATPase activity of NSF for SNARE complex disassembly and exocytosis.
    • Barnard RJO, Morgan A, Burgoyne RD. Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis. of special interest J Cell Biol. 139:1997;875-883 A mutation in α-SNAP results in a decreased ability to stimulate NSF ATPase activity. The mutant protein does not disassemble 20S SNARE complexes, but binds to NSF normally. In addition, this mutant does not stimulate exocytosis in permeabilized chromaffi cells, unlike wild-type α-SNAP. This study therefore emphasizes the role of α-SNAP in stimulating the ATPase activity of NSF for SNARE complex disassembly and exocytosis.
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    • Barnard, R.J.O.1    Morgan, A.2    Burgoyne, R.D.3
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    • The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin
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    • Hanson, P.I.1    Otto, H.2    Barton, N.3    Jahn, R.4
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    • Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
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    • Mayer, A.1    Wickner, W.2
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    • Sec18p (NSF)-driven release of Sec17p (α-SNAP) can precede docking and fusion of yeast vacuoles
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    • N-ethylmaleimide-sensitive factor-dependent α-SNAP release, an early event in the docking/fusion process, is not regulated by rab GTPases
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    • Colombo, M.I.1    Gelberman, S.C.2    Whiteheart, S.W.3    Stahl, P.D.4
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    • NSF and SNAP are present on adrenal chromaffin granules
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    • Burgoyne, R.D.1    Williams, G.2
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    • Steel, G.J.1    Tagaya, M.2    Woodman, P.G.3
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    • NSF is required for transport from early to late endosomes
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    • SNARE proteins - Why so many, why so few?
    • Linial M. SNARE proteins - why so many, why so few? J Neurochem. 69:1997;1781-1792.
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    • Regulation of neurotransmitter release kinetics by NSF
    • of special interest. This study analyzes the effect of peptides representing the D1 domain ??? NSF on neurotransmitter release in squid giant presynaptic terminals. Injection of certain peptides reduces the amount of neurotransmitter ??? and causes a small increase in the number of docked vesicles at active zone as well as a large decrease in the number of vesicles in the nerve terminal.
    • Schweizer FE, Dresbach T, DeBello WM, O'Conner V, Augustine GJ, Betz H. Regulation of neurotransmitter release kinetics by NSF. of special interest Science. 79:1998;1203-1206 This study analyzes the effect of peptides representing the D1 domain ??? NSF on neurotransmitter release in squid giant presynaptic terminals. Injection of certain peptides reduces the amount of neurotransmitter ??? and causes a small increase in the number of docked vesicles at active zone as well as a large decrease in the number of vesicles in the nerve terminal.
    • (1998) Science , vol.79 , pp. 1203-1206
    • Schweizer, F.E.1    Dresbach, T.2    Debello, W.M.3    O'Conner, V.4    Augustine, G.J.5    Betz, H.6
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    • Temperature-sensitive paralytic mutations demonstrate that assembly and disassembly of the SNARE complex are essential steps in neurotransmitter release
    • Temperature-sensitive paralytic mutations in Drosophila syntaxin and NS are characterized in this study. Syntaxin mutants at the nonpermissive temperature exhibit blocked synaptic transmission and fail to assemble ??? SNARE complexes. In contrast, mutations in NSF (comatose) also block synaptic transmission at the nonpermissive temperature but accumulate the t-SNARE syntaxin and 7S SNARE complexes on a light membrane ??? that contains SVs. The authors conclude that a cycle of SNARE ??? assembly and disassembly is essential for neurosecretion, and that NSF may be essential to disassemble SNARE complexes after fusion to allow additional cycles of fusion of special interest
    • Littleton TJ, Chapman ER, Kreber R, Garment MB, Carlson SD, Ganetzky B. Temperature-sensitive paralytic mutations demonstrate that assembly and disassembly of the SNARE complex are essential steps in neurotransmitter release. of special interest Neuron. 1998; Temperature-sensitive paralytic mutations in Drosophila syntaxin and NS are characterized in this study. Syntaxin mutants at the nonpermissive temperature exhibit blocked synaptic transmission and fail to assemble ??? SNARE complexes. In contrast, mutations in NSF (comatose) also block synaptic transmission at the nonpermissive temperature but accumulate the t-SNARE syntaxin and 7S SNARE complexes on a light membrane ??? that contains SVs. The authors conclude that a cycle of SNARE ??? assembly and disassembly is essential for neurosecretion, and that NSF may be essential to disassemble SNARE complexes after fusion to allow additional cycles of fusion.
    • (1998) Neuron
    • Littleton, T.J.1    Chapman, E.R.2    Kreber, R.3    Garment, M.B.4    Carlson, S.D.5    Ganetzky, B.6


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