Soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors (SNAREs) mediate vesicle fusion with the plasma membrane on activation by calcium binding to synaptotagmin. In the present study, we used fluorescence resonance energy transfer (FRET) and fluorescence lifetime imaging microscopy between fluorescently labeled SNARE proteins expressed in cultured rat hippocampal neuron...

Neuropeptide and peptide hormone secretion from neural and endocrine cells occurs by Ca(2+)-triggered dense-core vesicle exocytosis. The membrane fusion machinery consisting of vesicle and plasma membrane SNARE proteins needs to be assembled for Ca(2+)-triggered vesicle exocytosis. The related Munc13 and CAPS/UNC31 proteins that prime vesicle exocytosis are proposed to promote SNARE complex ass...

Intracellular membrane fusion mediates diverse processes including cell growth, division and communication. Fusion involves complex formation between SNARE proteins anchored to adjacent membranes. How and in what form interacting SNARE proteins reach their sites of action is virtually unknown. We have addressed this problem in the context of plant cell division in which a large number of TGN-de...

Target membrane proteins, SNAP-25 and syntaxin (t-SNARE), and secretory vesicleassociated membrane protein (v-SNARE), are part of the conserved protein complex involved in fusion of opposing bilayers in biological systems in the presence of calcium. It is known that SNARE interaction allows opposing bilayers to come close within a distance of approximately 3 Å, enabling calcium to drive membran...

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are required for intracellular membrane fusion, and are differentially localized throughout the cell. SNAREs on vesicle and target membranes contain "SNARE motifs" which interact to form a four-helix bundle that contributes to the fusion of two membranes. SNARE motif sequences fall into four classes, homologo...

Specific soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) proteins are required for different membrane transport steps. The SNARE Vti1a has been colocalized with Golgi markers and Vti1b with Golgi and the trans-Golgi network or endosomal markers in fibroblast cell lines. Here we study the distribution of Vti1a and Vti1b in brain. Vti1b was found in synaptic v...

Membrane-anchored SNAREs assemble into SNARE complexes that bring membranes together to promote fusion. SNARE complexes are parallel four-helix bundles stabilized in part by hydrophobic interactions within their core. At the center of SNARE complexes is a distinctive zero layer that consists of one arginine and three glutamines. This zero layer is thought to play a special role in the biology o...

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 comple...

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 comple...