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Redox regulation of Store Operated Ca2+ Entry

Published in Antioxidants & Redox Signaling. 2014, vol. 21, no. 6, p. 915-32
Abstract Significance: Store-operated Ca2+ entry (SOCE) is a ubiquitous Ca2+ signaling mechanism triggered by the Ca2+ depletion of the endoplasmic reticulum (ER) and by a variety of cellular stresses. Reactive oxygen species (ROS) are often concomitantly produced in response to these stresses, however the relationship between redox signaling and SOCE is not completely understood. Various cardiovascular, neurological and immune diseases are associated with alterations in both Ca2+ signaling and ROS production, thus understanding this relationship has therapeutic implications. Recent Advances: Several reactive cysteine modifications in STIM and Orai proteins comprising the core SOCE machinery were recently shown to modulate SOCE in a redox-dependent manner. Moreover, STIM1 and Orai1 expression levels may reciprocally regulate and be affected by responses to oxidative stress. ER proteins involved in oxidative protein folding have gained increased recognition as important sources of ROS, and the recent discovery of their accumulation in contact sites between the ER and mitochondria provides a further link between ROS production and intracellular Ca2+ handling. Critical Issues and future directions: Future research should aim to establish the complete set of SOCE controlling molecules, to determine their redox-sensitive residues, and to understand how intracellular Ca2+ stores dynamically respond to different types of stress. Mapping the precise nature and functional consequence of key redox-sensitive components of the pre- and post-translational control of SOCE machinery and of proteins regulating the ER calcium content will be pivotal in advancing our understanding of the complex cross-talk between redox and Ca2+ signaling.
PMID: 24053140
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NUNES-HASLER, Paula, DEMAUREX, Nicolas. Redox regulation of Store Operated Ca2+ Entry. In: Antioxidants & redox signaling, 2014, vol. 21, n° 6, p. 915-32. doi: 10.1089/ars.2013.5615 https://archive-ouverte.unige.ch/unige:32346

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Deposited on : 2013-12-18

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