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It is suggested that there is a regulatory Ca<jats:sup>2+<\/jats:sup>\u2010binding site on, or associated with, the luminal domain of the InsP<jats:sub>3<\/jats:sub> receptor, which allosterically controls Ca<jats:sup>2+<\/jats:sup> efflux, and the affinity for Ca<jats:sup>2+<\/jats:sup> of that site is modulated by InsP<jats:sub>3<\/jats:sub> binding to the cytoplasmic domain of the receptor; a similar mechanism applied to the ryanodine receptor might also explain some aspects of Ca<jats:sup>2+<\/jats:sup> \u2010induced Ca<jats:sup>2+<\/jats:sup> release. The stimulated entry of Ca<jats:sup>2+<\/jats:sup> into a cell which occurs upon activation of inositide\u2010linked receptors has been variously and confusingly proposed to be regulated by InsP<jats:sub>3<\/jats:sub>, InsP<jats:sub>4<\/jats:sub>, and\/or a \u2018capacitative\u2019 Ca<jats:sup>2+<\/jats:sup> pool; the mechanism of InsP, receptor action suggested here is shown to lead to a potential reconciliation of all these conflicting proposals.<\/jats:p>","DOI":"10.1016\/0014-5793(90)80692-c","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T07:44:17Z","timestamp":1027583057000},"page":"5-9","source":"Crossref","is-referenced-by-count":560,"title":["\u2018Quanta\u2019 Ca<sup>2+<\/sup> release and the control of Ca<sup>2+<\/sup> entry by inositol phosphates \u2010 a possible 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