v-SNARE transmembrane domains function as catalysts for vesicle fusion

• Published in: eLife Vol. 5
• Main Authors: Dhara, Madhurima, Yarzagaray, Antonio, Makke, Mazen, Schindeldecker, Barbara, Schwarz, Yvonne, Shaaban, Ahmed, Sharma, Satyan, Böckmann, Rainer A, Lindau, Manfred, Mohrmann, Ralf, Bruns, Dieter
• Format: Journal Article
• Language: English
• Published: England eLife Science Publications, Ltd 25.06.2016; eLife Sciences Publications Ltd; eLife Sciences Publications, Ltd
• Subjects: Amino acids; Animals; Biology; Calcium; Catalysts; Cells, Cultured; DNA Mutational Analysis; Exocytosis; Experiments; Flexibility; Isoleucine; Leucine; Lipids; Membrane Fusion; Membrane proteins; Mice; Models, Biological; Mutant Proteins - chemistry; Mutant Proteins - genetics; Mutant Proteins - metabolism; Mutation; Neuroscience; neurotransmitter release; Observations; Packaging; Physiological aspects; Protein Conformation; Protein structure; Protein-protein interactions; Proteins; Secretion; Secretory Vesicles - metabolism; SNAP receptors; Synaptobrevin; Transmembrane domains; Valine; Vesicle fusion; Vesicle-Associated Membrane Protein 2 - chemistry; Vesicle-Associated Membrane Protein 2 - genetics; Vesicle-Associated Membrane Protein 2 - metabolism; mouse; synaptobrevin; exocytosis; neurotransmitter release; neuroscience; membrane fusion

Vesicle fusion is mediated by an assembly of SNARE proteins between opposing membranes, but it is unknown whether transmembrane domains (TMDs) of SNARE proteins serve mechanistic functions that go beyond passive anchoring of the force-generating SNAREpin to the fusing membranes. Here, we show that c...