A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

Horikawa, Hiroshi; Saisu, Hideo; Ishizuka, Toru; Sekine, Yoko; Tsugita, Akira; Okada, Shoji; Abe, Teruo

doi:10.1016/0014-5793(93)80281-x

Cited by 80 publications

(39 citation statements)

References 29 publications

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“…Among them, rabphilin3A, originally described as a synaptic vesicle protein and recently identified in hormone secreting cells from various species [40], has been found to interact with rab3a and rab3c in a GTP-dependent manner [41,42]. The widely expressed protein rabin3 interacts with rab3a and rab3d (but not with rab3c) [43], whereas SNAP-25, VAMP/synaptobrevin-2, and syntaxins have been found to exist as a complex with rab3a in brain presynaptic terminals [44]. In addition, rab3a may also interact with SNARE [44,45] or the cytosolic protein doublet REEP-1 and -2 [23].…”

Section: Discussionmentioning

confidence: 99%

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

Garde

Roldán

1996

FEBS Letters

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Aerosomal exocytosis triggered with A23187/Ca 2+ was enhanced by rab3AL, a synthetic peptide corresponding to the effector domain of the small GTP-binding protein rab3. Exocytosis was further enhanced when spermatozoa were also exposed to dihutyryl-cAMP, but was prevented when H-89, a protein kinase A (PKA) inhibitor, was included. The action of rab3AL was not on, or upstream of, phospholipase A2 (PLA2). Inhibition of exocytosis by the PLA2 inhibitor aristolochic acid was overcome by rab3AL when it was included together with lysophosphatidylcholine; this effect was prevented by H-89. These results suggest a functional coupling between rab3 protein, metabolites generated by PLA2, and cAMP-activated PKA, in the final steps leading to membrane fusion during acrosomal exocytosis.Key words: Exocytosis; rab3; Phospholipase Az; Lysophosphatidylcholine; cAMP; Spermatozoa that regulate docking and fusion of secretory granules with the plasma membrane [16][17][18][19].Synthetic peptides corresponding to a putative effector domain of rab3 proteins have been shown to stimulate exocytosis in permeabilized [20 23] and intact cells [24], and membrane fusion in a cell-free assay system [25]. We have therefore used a sperm model system, where cells are stimulated to undergo exocytosis with A23187/Ca 2+, to explore whether rab3 might be involved in the final steps of membrane fusion during acrosomal exocytosis. We present, for the first time, evidence suggesting that rab3 protein, together with PLA2-derived metabolites and the cAMP/PKA signalling pathway, play an important role during the final steps of acrosomal exocytosis in mammalian spermatozoa. Materials and methods

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Section: Discussionmentioning

confidence: 99%

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

Garde

Roldán

1996

FEBS Letters

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“…Syntaxin 1 and SNAP-25 on the plasma membrane [15,35,36] and syntaxin 1 on chromaffin granules [27] can form a complex with VAMP-2. We examined whether or not SNAP-25 on chromaffin granules also forms a complex with VAMP-2 and syntaxin 1.…”

Section: Snap-25 On Chromaffin Granules Acts As a Snap Receptormentioning

confidence: 99%

SNAP‐25 is present on chromaffin granules and acts as a SNAP receptor

et al. 1996

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SNAP-25 is located on the plasma membrane and essential for exocytosis of neurotransmitters. It was suggested that SNAP-25 and syntaxin 1 via the interaction with VAMP-2 located on synaptic vesicles mediate the docking of the vesicles with the plasma membrane. In the present study, by means of biochemical and morphological analyses, we showed that SNAP-25 is present on chromaffin granules as well as on the plasma membrane. Reconstitution and immunoprecipitation analyses revealed that SNAP-25 on chromaffin granules has essentially the same properties as does SNAP-25 on the plasma membrane.

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“…Nerve terminals imaged by freeze fractu re exhibited large transmembrane particles at release sites (Pumplin et al, 1981;Heuser et al, 1974Heuser et al, , 1979Ceccarelli et al, 1979), which were believed to reflect the transmembrane regions of calcium channels. However, many other putative membrane proteins, including syntaxin (Bennett et al, 1992;O'Connor et al, 1993;Horikawa et al, 1993), neurexin (Petrenko et al, 1991;Petrenko, 1993), and calcium-activated potassium channels (Roberts et al, 1990;Robitaille et al, 1993), are also localized at or near the transmitter release site, and these may also generate particles in the freeze-fracture replica. Release face calcium channels can be identified with light microscopy, but the results obtained with AFM represent a 10-fold improvement in resolution, down to the molecular level.…”

Section: Analysis Of Calcium Channel Distributionmentioning

confidence: 99%

Localization of individual calcium channels at the release face of a presynaptic nerve terminal

Haydon

Henderson

Stanley

1994

Neuron

116

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SummaryStudies using biophysical techniques suggest a highly structured organization of calcium channels at the presynaptic transmitter release face (LEnds et al., 1981; Stanley, 1993), but it has not as yet proved possible to localize identified channels at the required nanometer level of resolution. We have used atomic force microscopy on the calyx-type nerve terminal of the chick ciliary ganglion to localize single calcium channels tagged via biotinylated ~o-conotoxin GVIA to avidin-coated 30 nm gold particles. Calcium channels were in low (modal value approximately ~ 1 per p,m ~) and high (modal value = 55 per l~m 2) density areas and exhibited a prominent interchannel spacing of 40 nm, indicating an intermolecular linkage. Particles were observed in clusters and short linear or parallel linear arrays, groupings that may reflect calcium channel organization at the transmitter release site.

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A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

Cited by 80 publications

References 29 publications

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

SNAP‐25 is present on chromaffin granules and acts as a SNAP receptor

Localization of individual calcium channels at the release face of a presynaptic nerve terminal

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A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

Cited by 80 publications

References 29 publications

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A2 metabolites

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A2 metabolites

SNAP‐25 is present on chromaffin granules and acts as a SNAP receptor

Localization of individual calcium channels at the release face of a presynaptic nerve terminal

Contact Info

Product

Resources

About

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites

rab3‐Peptide stimulates exocytosis of the ram sperm acrosome via interaction with cyclic AMP and phospholipase A₂ metabolites