Multiple SNARE interactions of an SM protein: Sed5p/Sly1p binding is dispensable for transport

@article{Peng2004MultipleSI,
  title={Multiple SNARE interactions of an SM protein: Sed5p/Sly1p binding is dispensable for transport},
  author={R. Peng and D. Gallwitz},
  journal={The EMBO Journal},
  year={2004},
  volume={23}
}
Sec1/Munc18 (SM) proteins are central to intracellular transport and neurotransmitter release but their exact role is still elusive. Several SM proteins, like the neuronal N‐Sec1 and the yeast Sly1 protein, bind their cognate t‐SNAREs with high affinity. This has been thought to be critical for their function. Here, we show that various mutant forms of Sly1p and the Golgi‐localized syntaxin Sed5p, which abolish their high‐affinity interaction, are fully functional in vivo, indicating that the… Expand
94 Citations
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