Abstract
Vesicle trafficking, a process essential to organelle biogenesis and secretion, requires the fusion of membranes. Most cellular membrane fusion occurs via the machinery of soluble N-ethylmaleimide sensitive factor (NSF) attachment protein receptor (SNARE) proteins, whose zippering catalyze the fusion of two opposing membranes. After the fusion event, the zippered (cis-)SNAREs are then disassembled by NSF in a step requiring ATP hydrolysis. To gain insights into the regulatory mechanism of SNARE assembly and disassembly, we engineered an intensity-based conformational sensor for SNAREs (icsenSNARE) by linking the structural transition of the SNARE complex to a fluorescence signal of cpGFP.
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