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. 1991 Jun 1;88(11):4911–4915. doi: 10.1073/pnas.88.11.4911

Structure-function relationships of the mouse inositol 1,4,5-trisphosphate receptor.

A Miyawaki 1, T Furuichi 1, Y Ryou 1, S Yoshikawa 1, T Nakagawa 1, T Saitoh 1, K Mikoshiba 1
PMCID: PMC51777  PMID: 1647021

Abstract

The homotetrameric complex of inositol 1,4,5-triphosphate (InsP3) receptors displays a Ca2+ release activity in response to InsP3 molecules. Structure-function relationships of the mouse cerebellar InsP3 receptor have been studied by analyses of a series of internal deletion or C-terminal truncation mutant proteins expressed in NG108-15 cells. Within the large cytoplasmic portion of the InsP3 receptor, approximately 650 N-terminal amino acids are highly conserved between mouse and Drosophila, and this region has the critical sequences for InsP3 binding that probably form the three-dimensionally restricted binding site. The N-terminal region of each InsP3 receptor subunit also binds one InsP3 molecule. Cross-linking experiments have revealed that InsP3 receptors are intermolecularly associated at the transmembrane domains and/or the successive C termini. The interaction between the receptor subunit and InsP3 may cause a conformational change in the tetrameric complex, resulting in the opening of Ca2+ channels.

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