期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 44, 期 -, 页码 452-459出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST20150233
关键词
calcium; endoplasmic reticulum (ER); inositol 1,4,5-trisphosphate receptor (IP3R); mitochondria-associated membrane (MAM); redox-dependent regulation; sarco/endoplasmic reticulum Ca2+ transport ATPase (SERCA); signal transduction
资金
- Canadian Cancer Society Research Institute [2010-700306]
- Cancer Research Society [18325]
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 Ero1 alpha with inositol 1,4,5-trisphosphate receptors (IP(3)Rs) 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.
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