Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and contribute to cell expansion, signaling, and polar growth in plants. The SNARE SYP121 of Arabidopsis thaliana that facilitates vesicle fusion at the plasma membrane also binds with, and regulates, K+ channels already present at the plasma membrane to affect K+ uptake a...

The N-ethylmaleimide-sensitive factor (NSF) and soluble NSF attachment protein (SNAP) are cytosolic factors that promote vesicle fusion with a target membrane in both the constitutive and regulated secretory pathways. NSF and SNAP are thought to function by catalyzing the disassembly of a SNAP receptor (SNARE) complex consisting of membrane proteins of the secretory vesicle and target membrane....

Although some of the principles of N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) function are well understood, remarkably little detail is known about sec1/munc18 (SM) protein function and its relationship to SNAREs. Popular models of SM protein function hold that these proteins promote or maintain an open and/or monomeric pool of syntaxin molecules available for SNARE c...

Genetic and biochemical evidence has established that a SNARE complex consisting of syntaxin 5 (Sed5)-mYkt6 (Ykt6)-GOS28 (Gos1)-GS15 (Sft1) is required for transport of proteins across the Golgi stack in animals (yeast). We have utilized quantitative immunogold labeling to establish the cis-trans distribution of the v-SNARE GS15 and the t-SNARE subunits GOS28 and syntaxin 5. Whereas the distrib...

nature of the interaction was not determined, tomosyn Tomosyn Binds t-SNARE Proteins was found to interact with the coiled coil domain of via a VAMP-like Coiled Coil syntaxin-1a. Furthermore, it was also suggested that tomosyn would be later replaced by VAMP to form the Exocytosis requires the fusion of vesicular and plasma SNARE complex required for membrane fusion, since the characterization ...

Synchronous neurotransmission depends on the tight coupling between Ca(2+) influx and fusion of neurotransmitter-filled vesicles with the plasma membrane. The vesicular soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein synaptobrevin 2 and the plasma membrane SNAREs syntaxin 1 and synaptosomal protein of 25 kDa (SNAP-25) are essential for calcium-triggered exo...

Viruses have a limited number of genes but a complex life cycle and have evolved to utilize numerous host factors to complete their replication. The assembly and budding process of enveloped viruses utilizes numerous cellular factors to facilitate transport from one membrane bound compartment to the other. The host SNARE proteins are widely involved in late stages of vesicular mediated transpor...

SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex formation between a vesicle and the target membrane is a central aspect of probably all vesicle fusion reactions. The sec1/munc18 (SM) protein family is also involved in membrane trafficking and fusion events. However, in contrast with the consensus on SNARE protein function, analysis of SM proteins in differe...

The trafficking of H+-ATPase vesicles to the apical membrane of inner medullary collecting duct (IMCD) cells utilizes a mechanism similar to that described in neurosecretory cells involving soluble N-ethylmaleimide-sensitive factor attachment protein target receptor (SNARE) proteins. Regulated exocytosis of these vesicles is associated with the formation of SNARE complexes. Clostridial neurotox...

The interaction between SM (Sec1/Munc18) and SNARE (soluble N-ethylmaleimide-sensitive factor-attachment receptor) proteins constitutes the core eukaryotic membrane fusion machinery which manages exocytosis by mediating fusion of constitutively exocytic vesicles with the plasma membrane. However, mechanistic details on the nature and the physiological impact of SM-SNARE interactions remain larg...