Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine.

Edelmann, Lambert; Hanson, Phyllis I.; Chapman, Edwin; Jahn, Reinhard

doi:10.1002/j.1460-2075.1995.tb06995.x

Cited by 418 publications

(367 citation statements)

References 58 publications

(66 reference statements)

Supporting

Mentioning

338

Contrasting

Unclassified

Order By: Relevance

“…As shown in Figure 7C, labeled syntaxin is only detectable in the synaptobrevin immunoprecipitates. As an independent readout for the synaptophysin-synaptobrevin complex, which avoids detergent solubilization, we used cross-linking using the bifunctional cross-linker DSS (Edelmann et al, 1995). Crosslinking resulted in the appearance of an additional band of ϳ55 kDa that was positive for both synaptophysin ( Figure 7D) and synaptobrevin (not shown).…”

Section: Synaptobrevin Dissociates From Synaptophysin Upon Snare Compmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Moreover, synaptobrevin is associated with synaptophysin, a major multispanning membrane protein of synaptic vesicles (Calakos and Scheller, 1994;Edelmann et al, 1995;Washbourne et al, 1995). This interaction appears to be mediated primarily by the transmembrane region of synaptobrevin (Edelmann et al, 1995;Yelamanchili et al, 2005). Interaction of synaptobrevin with synaptophysin and syntaxin 1/SNAP-25 is mutually exclusive (Edelmann et al, 1995), suggesting that release of synaptobrevin from synaptophysin may constitute an activation step.…”

Section: Introductionmentioning

confidence: 99%

“…Calmodulin was shown to compete with membrane binding of this region, and it was proposed that calmodulin binding inhibits rather than activates synaptobrevin (de Haro et al, 2004). Moreover, synaptobrevin is associated with synaptophysin, a major multispanning membrane protein of synaptic vesicles (Calakos and Scheller, 1994;Edelmann et al, 1995;Washbourne et al, 1995). This interaction appears to be mediated primarily by the transmembrane region of synaptobrevin (Edelmann et al, 1995;Yelamanchili et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…This interaction appears to be mediated primarily by the transmembrane region of synaptobrevin (Edelmann et al, 1995;Yelamanchili et al, 2005). Interaction of synaptobrevin with synaptophysin and syntaxin 1/SNAP-25 is mutually exclusive (Edelmann et al, 1995), suggesting that release of synaptobrevin from synaptophysin may constitute an activation step.Together, these reports suggest that the reactivity of synaptobrevin is controlled by protein and lipid interactions of its C-terminal region. However, recent experiments on fusion of synaptobrevin-containing liposomes are difficult to reconcile with the view of an intrinsic inactivation of the protein.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Determinants of Synaptobrevin Regulation in Membranes

Siddiqui

Vites

Stein³

et al. 2007

MBoC

View full text Add to dashboard Cite

Neuronal exocytosis is driven by the formation of SNARE complexes between synaptobrevin 2 on synaptic vesicles and SNAP-25/syntaxin 1 on the plasma membrane. It has remained controversial, however, whether SNAREs are constitutively active or whether they are down-regulated until fusion is triggered. We now show that synaptobrevin in proteoliposomes as well as in purified synaptic vesicles is constitutively active. Potential regulators such as calmodulin or synaptophysin do not affect SNARE activity. Substitution or deletion of residues in the linker connecting the SNARE motif and transmembrane region did not alter the kinetics of SNARE complex assembly or of SNARE-mediated fusion of liposomes. Remarkably, deletion of C-terminal residues of the SNARE motif strongly reduced fusion activity, although the overall stability of the complexes was not affected. We conclude that although complete zippering of the SNARE complex is essential for membrane fusion, the structure of the adjacent linker domain is less critical, suggesting that complete SNARE complex assembly not only connects membranes but also drives fusion. INTRODUCTIONCommunication between neurons is mediated by neurotransmitters that are released from presynaptic nerve endings by Ca 2ϩ -dependent exocytosis of synaptic vesicles. Exocytotic fusion of the vesicle with the synaptic plasma membrane is mediated by the proteins synaptobrevin 2/VAMP2, SNAP-25, and syntaxin 1 (Jahn and Scheller, 2006;Rizo et al., 2006). These proteins are members of the SNARE protein family that are involved in all fusion events of the secretory pathway. SNAREs are characterized by stretches of 60-70 amino acids arranged in heptad repeats, termed SNARE motifs (Weimbs et al., 1997;Fasshauer et al., 1998b;Bock et al., 2001;Day et al., 2006). Syntaxin and synaptobrevin each contain a single SNARE motif that is located adjacent to a C-terminal transmembrane domain. In contrast, SNAP-25 contains two SNARE motifs connected by a palmitoylated linker region that serves as membrane anchor.Synaptobrevin resides in synaptic vesicles, whereas SNAP-25 and syntaxin 1 reside in the plasma membrane. The SNARE motifs of syntaxin, SNAP-25, and synaptobrevin readily assemble into quarternary bundles of ␣-helices (Fasshauer et al., 1997;Sutton et al., 1998). Assembly would thus lead to a tight connection between the membranes. According to this view, assembly is nucleated at the Nterminal ends of the SNARE-motifs and proceeds toward the C-terminal membrane anchor ("zippering"), resulting in a strained "trans"-complex . During membrane merger, the trans-complex would relax into a "cis"-complex in which the transmembrane domains are aligned in parallel. To regenerate the SNAREs for another round of fusion, SNARE complexes need to be disassembled by the AAAϩ-ATPase NEM-sensitive factor (NSF) in conjunction with cofactors termed soluble NSF attachment proteins (SNAPs; Sollner et al., 1993).Although the "zippering" hypothesis of SNARE function has received a lot of experimental support, it is still unclear...

show abstract

Section: Synaptobrevin Dissociates From Synaptophysin Upon Snare Compmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Determinants of Synaptobrevin Regulation in Membranes

Siddiqui

Vites

Stein³

et al. 2007

MBoC

View full text Add to dashboard Cite

show abstract

Increased Concentrations of Presynaptic Proteins in the Cingulate Cortex of Subjects With Schizophrenia

Gabriel

Haroutunian²,

Powchih³

et al. 1997

Arch Gen Psychiatry

127

View full text Add to dashboard Cite

show abstract

Differential synaptic vesicle protein expression in the barrel field of developing cortex

Stettler¹,

Tavitian²,

Moya³

1996

J. Comp. Neurol.

View full text Add to dashboard Cite

The distribution of four proteins associated with synaptic vesicles, SV2, synaptophysin, synapsin I, and rab3a, was investigated during postnatal development of the posteromedial barrel subfield (PMBSF) in the rat somatosensory cortex. A distinct progression in the appearance of the different synaptic vesicle proteins within the PMBSF was observed. SV2, synapsin I, and synaptophysin revealed the organization of the barrel field in the neonate. This early demarcation of the cortical representation of the vibrissal array coincides with the earliest known age for the emergence of the cytoarchitectonic organization of this region. In contrast, rab3a did not delimit the barrels until the end of the 1st postnatal week, coincident with the known onset of adult-like physiological activity and the loss of plasticity in afferents to this region. In addition, the appearance of the different synaptic vesicle proteins occurred earlier within the PMBSF than in the adjacent extra-barrel regions of the cortex. These results show that the molecular differentiation of synaptic fields across the cortex is not a homogeneous and synchronous process in terms of synaptic vesicle protein expression. Because these proteins act together in mature synapses to ensure the regulated release of neurotransmitters, our results suggest that this temporo-spatial asynchrony may underlie different potentials for synaptic activity and thus contribute to the development of cortical maps.

show abstract

Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine.

Cited by 418 publications

References 58 publications

Determinants of Synaptobrevin Regulation in Membranes

Determinants of Synaptobrevin Regulation in Membranes

Increased Concentrations of Presynaptic Proteins in the Cingulate Cortex of Subjects With Schizophrenia

Differential synaptic vesicle protein expression in the barrel field of developing cortex

Contact Info

Product

Resources

About