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lüll IP(3) receptors: toward understanding their activation Taylor CW; Tovey SCCold Spring Harb Perspect Biol 2010[Dec]; 2 (12): a004010Inositol 1,4,5-trisphosphate receptors (IP(3)R) and their relatives, ryanodine receptors, are the channels that most often mediate Ca(2+) release from intracellular stores. Their regulation by Ca(2+) allows them also to propagate cytosolic Ca(2+) signals regeneratively. This brief review addresses the structural basis of IP(3)R activation by IP(3) and Ca(2+). IP(3) initiates IP(3)R activation by promoting Ca(2+) binding to a stimulatory Ca(2+)-binding site, the identity of which is unresolved. We suggest that interactions of critical phosphate groups in IP(3) with opposite sides of the clam-like IP(3)-binding core cause it to close and propagate a conformational change toward the pore via the adjacent N-terminal suppressor domain. The pore, assembled from the last pair of transmembrane domains and the intervening pore loop from each of the four IP(3)R subunits, forms a structure in which a luminal selectivity filter and a gate at the cytosolic end of the pore control cation fluxes through the IP(3)R.|*Models, Molecular[MESH]|*Protein Conformation[MESH]|Binding Sites/genetics[MESH]|Calcium Signaling/*physiology[MESH]|Calcium/*metabolism[MESH]|Inositol 1,4,5-Trisphosphate Receptors/*metabolism[MESH]|Phosphates/metabolism[MESH]|Ryanodine Receptor Calcium Release Channel/*metabolism[MESH] |