Distribution and expression of SNAP-25 immunoreactivity in rat brain, rat PC-12 cells and human SMS-KCNR neuroblastoma cells

Oyler, George A.; Polli, Joseph W.; Higgins, Gerald A.; Wilson, Michael C.; Billingsley, Melvin L.

doi:10.1016/0165-3806(92)90172-s

Cited by 48 publications

(21 citation statements)

References 17 publications

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“…1B) and also confirmed, using a different antibody than employed elsewhere, its presence in PC12 and cultured chromaffin cells, as recently reported [19,20]. Its electrophoretic migration was identical to that of the band detected in cerebellar extracts (lane d; Fig.…”

Section: Snap-25 Dbhsupporting

confidence: 63%

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SNAP‐25 is differentially expressed by noradrenergic and adrenergic chromaffin cells

et al. 1996

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Section: Snap-25 Dbhsupporting

confidence: 63%

“…SNAP-25 has been shown to be present in PC12 tumour cells derived from adrenal medulla [19] and its presence in cultured chromaffin cells was reported while the present study was in progress [20]. In addition a possible role of SNAP-25 in secretion in chromaffin cells has been proposed [21,22].…”

Section: Introductionmentioning

confidence: 97%

SNAP‐25 is differentially expressed by noradrenergic and adrenergic chromaffin cells

et al. 1996

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“…is localized predominately at the plasma membrane in neurons and neuronal cell lines (21,22). To determine if GFP could be used as a reporter to characterize the membrane-targeting domain of SNAP-25, we constructed a fusion protein with full-length SNAP-25 fused to GFP (Fig.…”

Section: Full-length Snap-25 Targets Gfp To the Plasma Membrane-snap-25mentioning

confidence: 99%

SNAP-25 Is Targeted to the Plasma Membrane through a Novel Membrane-binding Domain

Gonzalo

Greentree

Linder

1999

Journal of Biological Chemistry

109

115

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SNAP-25, syntaxin, and synaptobrevin are SNARE proteins that mediate fusion of synaptic vesicles with the plasma membrane. Membrane attachment of syntaxin and synaptobrevin is achieved through a C-terminal hydrophobic tail, whereas SNAP-25 association with membranes appears to depend upon palmitoylation of cysteine residues located in the center of the molecule. This process requires an intact secretory pathway and is inhibited by brefeldin A. Here we show that the minimal plasma membrane-targeting domain of SNAP-25 maps to residues 85-120. This sequence is both necessary and sufficient to target a heterologous protein to the plasma membrane. Palmitoylation of this domain is sensitive to brefeldin A, suggesting that it uses the same membranetargeting mechanism as the full-length protein. As expected, the palmitoylated cysteine cluster is present within this domain, but surprisingly, membrane anchoring requires an additional five-amino acid sequence that is highly conserved among SNAP-25 family members. Significantly, the membrane-targeting module coincides with the protease-sensitive stretch (residues 83-120) that connects the two ␣-helices that SNAP-25 contributes to the four-helix bundle of the synaptic SNARE complex. Our results demonstrate that residues 85-120 of SNAP-25 represent a protein module that is physically and functionally separable from the SNARE complexforming domains.Intracellular membrane trafficking depends on specific interactions between vesicles and target membranes. Biochemical and genetic studies demonstrate that integral membrane proteins referred to as SNAREs (soluble N-ethylmaleimidesensitive factor attachment protein receptors) are important elements in this process (1, 2). The best characterized SNARE proteins are those that mediate synaptic vesicle exocytosis in nerve terminals (reviewed in Ref.3). SNAP-25 (synaptosomeassociated protein of 25 kDa) and syntaxin are plasma membrane proteins that bind to the synaptic vesicle protein, synaptobrevin/vesicle-associated membrane protein. The critical role that these proteins play in neurotransmission is underscored by the fact that all three are targets of tetanus or botulinum neurotoxins that block neurotransmitter release.SNAP-25, syntaxin, and synaptobrevin bind to each other to form a stable heterotrimeric complex that consists of a fourhelix bundle (4, 5). SNAP-25 contributes two helices from its Nand C-terminal domains; syntaxin and synaptobrevin each provide one. Syntaxin and synaptobrevin are anchored in opposing membranes through transmembrane domains at their C termini. The parallel orientation of these membrane-anchored helices within the complex has led to a model in which the zippering action of complex formation brings the membranes together, with the energy of complex formation driving membrane fusion (6 -8). However, whether SNARE proteins directly mediate fusion remains uncertain (9). Unlike synaptobrevin and syntaxin, SNAP-25 is associated with membranes through palmitoylated cysteines found near the center of the molecul...

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“…En utilisant SNAP et NSF comme appât, ils ont isolés trois protéines à partir d'un extrait de cerveau bovin, qu'ils ont appelées SNARE (pour SNAP receptors) [7]. Ces trois protéines avaient déjà été identifiées, entre autres par De Camilli, Jahn, Scheller et Südhof, comme des protéines abondantes de la terminaison présynaptique : Synaptobrevine 2/VAMP2, Syntaxine 1 et SNAP-25 [8][9][10], mais leur fonction exacte était inconnue. Comme Synaptobrevine est localisée dans les vésicules synaptiques, tandis que Syntaxine réside dans la membrane plasmique présynaptique, J. Rothman a proposé la fameuse « hypothèse SNARE » selon laquelle une vésicule de transport s'accroche et fusionne avec une membrane cible lorsqu'une protéine v-SNARE de la vésicule interagit avec une protéine t-SNARE de la membrane cible (target) (Figure 1).…”

Section: L'hypothèse Snareunclassified

Une récompense pour la découverte des acteurs et des mécanismes moléculaires fondamentaux du trafic vésiculaire intracellulaire

2013

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Distribution and expression of SNAP-25 immunoreactivity in rat brain, rat PC-12 cells and human SMS-KCNR neuroblastoma cells

Cited by 48 publications

References 17 publications

SNAP‐25 is differentially expressed by noradrenergic and adrenergic chromaffin cells

SNAP‐25 is differentially expressed by noradrenergic and adrenergic chromaffin cells

SNAP-25 Is Targeted to the Plasma Membrane through a Novel Membrane-binding Domain

Une récompense pour la découverte des acteurs et des mécanismes moléculaires fondamentaux du trafic vésiculaire intracellulaire

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