An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage.

@article{Ando2009AnIH,
  title={An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage.},
  author={Hideaki Ando and Akihiro Mizutani and Katsuhiko Mikoshiba},
  journal={Journal of neurochemistry},
  year={2009},
  volume={109 2},
  pages={
          539-50
        }
}
IRBIT is an inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R)-binding protein that inhibits the activation of IP(3)R by competing with IP(3) for the common binding site on IP(3)R. In this study, we characterize an IRBIT homologue, termed Long-IRBIT. Long-IRBIT is highly homologous to IRBIT ( approximately 88%) and heteromerizes with IRBIT. In spite of complete conservation of critical amino acids required for the interaction with IP(3)R and comparable phosphorylations on critical four Ser… CONTINUE READING

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