Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate.

@article{Rickman2004SynaptotagminIW,
  title={Synaptotagmin interaction with the syntaxin/SNAP-25 dimer is mediated by an evolutionarily conserved motif and is sensitive to inositol hexakisphosphate.},
  author={Colin Rickman and Deborah A Archer and Fr{\'e}d{\'e}ric A Meunier and Molly Craxton and Mitsunori Fukuda and Robert D. Burgoyne and Bazbek A. Davletov},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 13},
  pages={12574-9}
}
Synaptotagmins are membrane proteins that possess tandem C2 domains and play an important role in regulated membrane fusion in metazoan organisms. Here we show that both synaptotagmins I and II, the two major neuronal isoforms, can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25) dimer, the immediate precursor of the soluble NSF attachment protein receptor (SNARE) fusion complex. A stretch of basic amino acids highly conserved throughout the animal kingdom is… CONTINUE READING

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Coupling of Synaptotagmins I and II to t-SNARE Dimer 12579 by gest on N ovem er 9, 2016 hp://w w w .jb.org/ D

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