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- W2312550217 endingPage "459" @default.
- W2312550217 startingPage "452" @default.
- W2312550217 abstract "The endoplasmic reticulum (ER) is the main cellular Ca2+ storage unit. Among other signalling outputs, the ER can release Ca2+ ions, which can, for instance, communicate the status of ER protein folding to the cytosol and to other organelles, in particular the mitochondria. As a consequence, ER Ca2+ flux can alter the apposition of the ER with mitochondria, influence mitochondrial ATP production or trigger apoptosis. All aspects of ER Ca2+ flux have emerged as processes that are intimately controlled by intracellular redox conditions. In this review, we focus on ER-luminal redox-driven regulation of Ca2+ flux. This involves the direct reduction of disulfides within ER Ca2+ handling proteins themselves, but also the regulated interaction of ER chaperones and oxidoreductases such as calnexin or ERp57 with them. Well-characterized examples are the activating interactions of Ero1α with inositol 1,4,5-trisphosphate receptors (IP3Rs) or of selenoprotein N (SEPN1) with sarco/endoplasmic reticulum Ca2+ transport ATPase 2 (SERCA2). The future discovery of novel ER-luminal modulators of Ca2+ handling proteins is likely. Based on the currently available information, we describe how the variable ER redox conditions govern Ca2+ flux from the ER." @default.
- W2312550217 created "2016-06-24" @default.
- W2312550217 creator A5005161224 @default.
- W2312550217 creator A5030346632 @default.
- W2312550217 date "2016-04-11" @default.
- W2312550217 modified "2023-09-25" @default.
- W2312550217 title "ER-luminal thiol/selenol-mediated regulation of Ca2+ signalling" @default.
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- W2312550217 doi "https://doi.org/10.1042/bst20150233" @default.