Analysis of IP3 receptors in and out of cells

Autor: Ana M. Rossi, Taufiq Rahman, Stephen C. Tovey, David L. Prole, Colin W. Taylor
Rok vydání: 2012
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - General Subjects. 1820:1214-1227
ISSN: 0304-4165
Popis: Background Inositol 1,4,5-trisphosphate receptors (IP 3 R) are expressed in almost all animal cells. Three mammalian genes encode closely related IP 3 R subunits, which assemble into homo- or hetero-tetramers to form intracellular Ca 2 + channels. Scope of the review In this brief review, we first consider a variety of complementary methods that allow the links between IP 3 binding and channel gating to be defined. How does IP 3 binding to the IP 3 -binding core in each IP 3 R subunit cause opening of a cation-selective pore formed by residues towards the C-terminal? We then describe methods that allow IP 3 , Ca 2 + signals and IP 3 R mobility to be examined in intact cells. A final section briefly considers genetic analyses of IP 3 R signalling. Major conclusions All IP 3 R are regulated by both IP 3 and Ca 2 + . This allows them to initiate and regeneratively propagate intracellular Ca 2 + signals. The elementary Ca 2 + release events evoked by IP 3 in intact cells are mediated by very small numbers of active IP 3 R and the Ca 2 + -mediated interactions between them. The spatial organization of these Ca 2 + signals and their stochastic dependence on so few IP 3 Rs highlight the need for methods that allow the spatial organization of IP 3 R signalling to be addressed with single-molecule resolution. General significance A variety of complementary methods provide insight into the structural basis of IP 3 R activation and the contributions of IP 3 -evoked Ca 2 + signals to cellular physiology. This article is part of a Special Issue entitled Biochemical, biophysical and genetic approaches to intracellular calcium signaling.
Databáze: OpenAIRE
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