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={Renwang Peng and Dieter Gallwitz},
  journal={The EMBO journal},
  year={2004},
  volume={23 20},
  pages={
          3939-49
        }
}
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… CONTINUE READING

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