PRIP (phospholipase C-related but catalytically inactive protein) inhibits exocytosis by direct interactions with syntaxin 1 and SNAP-25 through its C2 domain.

@article{Zhang2013PRIPC,
  title={PRIP (phospholipase C-related but catalytically inactive protein) inhibits exocytosis by direct interactions with syntaxin 1 and SNAP-25 through its C2 domain.},
  author={Zhao Zhang and Hiroshi Takeuchi and Jing Gao and DaGuang Wang and Declan J. James and Thomas F J Martin and Masato Hirata},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 11},
  pages={7769-80}
}
Membrane fusion for exocytosis is mediated by SNAREs, forming trans-ternary complexes to bridge vesicle and target membranes. There is an array of accessory proteins that directly interact with and regulate SNARE proteins. PRIP (phospholipase C-related but catalytically inactive protein) is likely one of these proteins; PRIP, consisting of multiple functional modules including pleckstrin homology and C2 domains, inhibited exocytosis, probably via the binding to membrane phosphoinositides… CONTINUE READING
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