Structural basis for the inhibitory role of tomosyn in exocytosis.

@article{Pobbati2004StructuralBF,
  title={Structural basis for the inhibitory role of tomosyn in exocytosis.},
  author={Ajaybabu V. Pobbati and Adelia Razeto and Matthias B{\"o}ddener and Stefan Becker and Dirk Fasshauer},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 45},
  pages={47192-200}
}
Upon Ca2+ influx synaptic vesicles fuse with the plasma membrane and release their neurotransmitter cargo into the synaptic cleft. Key players during this process are the Q-SNAREs syntaxin 1a and SNAP-25 and the R-SNARE synaptobrevin 2. It is thought that these membrane proteins gradually assemble into a tight trans-SNARE complex between vesicular and plasma membrane, ultimately leading to membrane fusion. Tomosyn is a soluble protein of 130 kDa that contains a COOH-terminal R-SNARE motif but… CONTINUE READING

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Structure of the Tomosyn SNARE Complex 47200 at M ax P lanck Ist.B iophikalische C em ,O tto H hn B il,P f.2841,37018 G oeingen on M arch 23

  • C. H. Widberg, N. J. Bryant, M. Girotti, S. Rea, D. E. James
  • J. Biol. Chem. 278,
  • 2003
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