Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes

• DOI: 10.1083/jcb.200202006
• Publication Date: 2002-07-26T16:48:16Z
• Authors: Renwang Peng; Dieter Gallwitz
• Keywords: SNARE complex; Vesicular Transport Proteins; Vesicle fusion; Munc-18; Syntaxin 3

Fusion of transport vesicles with their target organelles involves specific membrane proteins, SNAREs, which form tight complexes bridging the membranes to be fused. Evidence from yeast and mammals indicates that Sec1 family proteins act as regulators fusion by binding SNAREs. In experiments purified we now made observation ER Golgi core SNARE complex could assembled on syntaxin Sed5p tightly bound Sec1-related Sly1p. Sly1p also preassembled in vitro was found part a vesicular/target immunoprecipitated cell lysates. This is marked contrast exocytic assembly neuronal cells where high affinity N-Sec1/Munc-18 1A precluded formation. We kinetics formation either Sly1p-bound or free not significantly different. Importantly, several presumably nonphysiological easily generated did when first for time member contributes specificity assembly.