CaBP1, a neuronal Ca2+ sensor protein, inhibits inositol trisphosphate receptors by clamping intersubunit interactions.

@article{Li2013CaBP1AN,
  title={CaBP1, a neuronal Ca2+ sensor protein, inhibits inositol trisphosphate receptors by clamping intersubunit interactions.},
  author={Congmin Li and Masahiro Enomoto and Ana Carolina Marinho Rossi and Min-duk Seo and Taufiq Rahman and Peter B Stathopulos and Colin W Taylor and Mitsuhiko Ikura and James B Ames},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 21},
  pages={
          8507-12
        }
}
Calcium-binding protein 1 (CaBP1) is a neuron-specific member of the calmodulin superfamily that regulates several Ca(2+) channels, including inositol 1,4,5-trisphosphate receptors (InsP3Rs). CaBP1 alone does not affect InsP3R activity, but it inhibits InsP3-evoked Ca(2+) release by slowing the rate of InsP3R opening. The inhibition is enhanced by Ca(2+) binding to both the InsP3R and CaBP1. CaBP1 binds via its C lobe to the cytosolic N-terminal region (NT; residues 1-604) of InsP3R1. NMR… CONTINUE READING

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