Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif.

@article{Yamaguchi2002Sly1BT,
  title={Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif.},
  author={Tomohiro Yamaguchi and Irina Dulubova and Sang-Won Min and Xiaocheng Chen and Josep Rizo and Thomas C S{\"u}dhof},
  journal={Developmental cell},
  year={2002},
  volume={2 3},
  pages={295-305}
}
Sec1/munc18-like proteins (SM proteins) and SNARE complexes are probably universally required for membrane fusion. However, the molecular mechanism by which they interact has only been defined for synaptic vesicle fusion where munc18 binds to syntaxin in a closed conformation that is incompatible with SNARE complex assembly. We now show that Sly1, an SM protein involved in Golgi and ER fusion, binds to a short, evolutionarily conserved N-terminal peptide of Sed5p and Ufe1p in yeast and of… CONTINUE READING
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