Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins.

@article{Dulubova2003ConvergenceAD,
  title={Convergence and divergence in the mechanism of SNARE binding by Sec1/Munc18-like proteins.},
  author={Irina Dulubova and Tomohiro Yamaguchi and Demet Araç and Hongmei Li and Iryna Huryeva and Sang-Won Min and Josep Rizo and Thomas C. Sudhof},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 1},
  pages={32-7}
}
Sec1Munc18-like (SM) proteins functionally interact with soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) in membrane fusion, but the mechanisms of these interactions differ. In vertebrates, SM proteins that mediate exocytosis (Munc18-1, 18-2, and 18c) bind to the closed conformation of syntaxins 1-4, which requires the N-terminal H(abc) domains and SNARE motifs of these syntaxins. In contrast, SM proteins that mediate Golgi and endoplasmic reticulum fusion (Sly1… CONTINUE READING