Regulation of Ins(1,4,5)P3 receptor isoforms by endogenous modulators.
Three isoforms of the inositol (1,4,5)-trisphosphate [Ins(1,4,5)P3] receptor have been identified. Each receptor isoform has been functionally characterized using many different techniques. Although these receptor isoforms possess high homology, interesting differences in their Ca2+ dependence, Ins(1,4,5)P3 sensitivity and subcellular distribution exist, implying distinct cellular roles. Indeed, interplay among the isoforms might be necessary for a cell to control spatial and temporal aspects of cytosolic Ca2+ signals, which are important for many cellular processes. In this review isoform-specific functions, primarily at the single-channel level, will be highlighted and these properties will be correlated with Ca2+ signals in intact cells.
Thrower
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Dept of Pharmacology, Yale University, PO Box 208066, 333 Cedar Street, New Haven, CT 06520-8066, USA. edwin.thrower@yale.edu
Hagar
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Ehrlich
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D000818:Animals; D015220:Calcium Channels / Q000187:drug effects / Q000502:physiology*; D006801:Humans; D053496:Inositol 1,4,5-Trisphosphate Receptors; D010766:Phosphorylation; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D018160:Receptors, Cytoplasmic and Nuclear / Q000187:drug effects / Q000502:physiology*
D015220:Calcium Channels; C506926:ITPR1 protein, human; D053496:Inositol 1,4,5-Trisphosphate Receptors; D011956:Receptors, Cell Surface; D018160:Receptors, Cytoplasmic and Nuclear