SNARE Complex Oligomerization by Synaphin/Complexin Is Essential for Synaptic Vesicle Exocytosis

Tokumaru, Hiroshi; Umayahara, Keiko; Pellegrini, Lorenzo; Ishizuka, Toru; Saisu, Hideo; Betz, Heinrich; Augustine, George J; Abe, Teruo

doi:10.1016/s0092-8674(01)00229-x

Cited by 147 publications

(132 citation statements)

References 59 publications

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“…Munc18a and Munc13-1 have been shown to be "priming" factors that increase the release potential for a given population of vesicles (Ashery et al, 2000;Voets et al, 2001). Complexins are also purported to play a role in SNARE complex assembly and stabilization (Reim et al, 2001;Tokumaru et al, 2001). Though a dysfunction in any of these proteins could lead to an increase in SNARE complexes, no alterations in their levels were detected in the amygdalar kindled animals (Table 3).…”

Section: Discussionmentioning

confidence: 99%

“…The five bands representing 7S SNARE complexes (bands indicated in Fig. 1A) may be SNARE oligomers, as suggested by (Tokumaru et al, 2001). These bands were quantified and their sum was considered the total 7S SNARE complex in that synaptosomal preparation.…”

Section: Kindling Increases 7s Snare Complexes In Hippocampal Synaptomentioning

confidence: 99%

“…Munc13 proteins are priming factors that promote the formation of the "readily releasable pool" of secretory vesicles (Ashery et al, 2000). Complexins compete with α-SNAP for SNARE complex binding and affect SNARE complex stability (Hu et al, 2002;Tokumaru et al, 2001). Synaptotagmins are potential calcium sensors that regulate the final steps of membrane fusion (Yoshihara et al, 2003).…”

Section: Analysis Of Other Secretory Machinery Proteinsmentioning

confidence: 99%

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Asymmetric accumulation of hippocampal 7S SNARE complexes occurs regardless of kindling paradigm

et al. 2007

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Modifications of neurotransmission may contribute to the synchronization of neuronal networks that are a hallmark of epileptic seizures. In this study we examine the synaptosomal proteins involved in neurotransmitter release to determine if alterations in their interactions correlate with the chronic epileptic state. Using quantitative western blotting, we measured the levels of 7S SNARE complexes and SNARE effectors in the effected hippocampi from animals that were electrically kindled through stimulation from one of three different foci. All three kindling paradigms, amygdalar, entorhinal, and septal, were associated with an accumulation of 7S SNARE complexes in the ipsilateral hippocampus, measured one month after completion of kindling. Of the eight SNARE effectors examined (α-SNAP, NSF, SV2A/B, Munc18a/nSec1, Munc13-1, Complexin 1, 2, and synaptotagmin I), there was a statistically significant bihemispheric increase of hippocampal SV2 and decrease of NSF upon kindling; neither by itself would be expected to account for the asymmetry of SNARE complex distribution. These data suggest that an ipsilateral hippocampal accumulation of SNARE complexes is a permanent alteration of kindling-induced epilepsy, regardless of stimulation pathway. The significance of these findings toward a molecular understanding of epilepsy will be discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Kindling Increases 7s Snare Complexes In Hippocampal Synaptomentioning

confidence: 99%

Section: Analysis Of Other Secretory Machinery Proteinsmentioning

confidence: 99%

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Asymmetric accumulation of hippocampal 7S SNARE complexes occurs regardless of kindling paradigm

et al. 2007

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“…To establish whether binding partners of complexins were present (Tokumaru et al, 2001), the distribution of syntaxin-1 was determined in rabbit retina. Syntaxin-1 immunoreactivity was robust in the IPL and outlined numerous amacrine cell bodies in the proximal INL (Fig.…”

Section: Syntaxin-1mentioning

confidence: 99%

Cellular distribution and subcellular localization of molecular components of vesicular transmitter release in horizontal cells of rabbit retina

Hirano

Brandstätter

Brecha

2005

J of Comparative Neurology

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The mechanism underlying transmitter release from retinal horizontal cells is poorly understood. We investigated the possibility of vesicular transmitter release from mammalian horizontal cells by examining the expression of synaptic proteins that participate in vesicular transmitter release at chemical synapses. Using immunocytochemistry, we evaluated the cellular and subcellular distribution of complexin I/II, syntaxin-1, and synapsin I in rabbit retina. Strong labeling for complexin I/II, proteins that regulate a late step in vesicular transmitter release, was found in both synaptic layers of the retina, and in somata of A-and B-type horizontal cells, of ␥-aminobutyric acid (GABA)-and glycinergic amacrine cells, and of ganglion cells. Immunoelectron microscopy demonstrated the presence of complexin I/II in horizontal cell processes postsynaptic to rod and cone ribbon synapses. Syntaxin-1, a core protein of the soluble N-ethylmaleimide-sensitive-factor attachment protein receptor (SNARE) complex known to bind to complexin, and synapsin I, a synaptic vesicle-associated protein involved in the Ca 2ϩ -dependent recruitment of synaptic vesicles for transmitter release, were also present in the horizontal cells and their processes at photoreceptor synapses. Photoreceptors and bipolar cells did not express any of these proteins at their axon terminals. The presence of complexin I/II, syntaxin-1, and synapsin I in rabbit horizontal cell processes and tips suggests that a vesicular mechanism may underlie transmitter release from mammalian horizontal cells.

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“…Initial studies suggested that multimerization of synaptic SNARE complexes could be achieved via domain swapping, whereby one of the two SNAP-25 helices could be substituted by the equivalent helix from a neighboring complex (Kweon et al, 2002). Alternative models proposed the involvement of accessory proteins, such as synaptotagmin (Littleton et al, 2001) or complexin (Tokumaru et al, 2001), or the transmembrane domains of syb2 and syntaxin 1A (Laage et al, 2000), in synaptic SNARE complex multimerization. However, SNARE complexes assembled from recombinant coils and lacking transmembrane domains are able to associate with each other (Fasshauer et al, 1997;Fasshauer et al, 1998;Margittai et al, 2001;Ernst and Brü nger, 2003), arguing that at least some of the interactions that support multimerization may require neither accessory proteins nor transmembrane domains.…”

Section: Introductionmentioning

confidence: 99%

A Role for Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor Complex Dimerization during Neurosecretion

Fdez

Jowitt

Wang

et al. 2008

MBoC

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The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C termini of cytosolic SNARE complexes are in apposition, and it involves residues from the vesicleassociated SNARE synaptobrevin 2 that lie close to the cytosol-membrane interface within the full-length protein.Mutation of these residues reduces stability of dimers formed between SNARE complexes, without affecting the stability of each individual SNARE complex. These mutations also cause a corresponding decrease in the ability of botulinum toxin-resistant synaptobrevin 2 to rescue regulated exocytosis in toxin-treated neuroendocrine cells. Moreover, such synaptobrevin 2 mutants give rise to a dominant-negative inhibition of exocytosis. These data are consistent with an important role for SNARE complex dimers in neurosecretion.

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SNARE Complex Oligomerization by Synaphin/Complexin Is Essential for Synaptic Vesicle Exocytosis

Cited by 147 publications

References 59 publications

Asymmetric accumulation of hippocampal 7S SNARE complexes occurs regardless of kindling paradigm

Asymmetric accumulation of hippocampal 7S SNARE complexes occurs regardless of kindling paradigm

Cellular distribution and subcellular localization of molecular components of vesicular transmitter release in horizontal cells of rabbit retina

A Role for Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor Complex Dimerization during Neurosecretion

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