IRE1α Signaling Pathways Involved in Mammalian Cell Fate Determination

Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology
Jie WuQiao-Bing Huang

Abstract

A diverse array of cellular stresses can lead to accumulation of misfolded or unfolded proteins in endoplasmic reticulum (ER), which subsequently elicits ER stress. Inositol-requiring enzyme 1α (IRE1α) is the most sensitive of the three unfolded protein response (UPR) branches which are triggered to cope with ER stress in mammalian cells. IRE1α signaling is quite context-specific on account of many adaptor and modulator proteins that directly interact with it, including heat shock proteins (HSPs), RING finger protein 13 (RNF13), poly (ADP-ribose) polymerase 16 (PARP16), Bax/Bak, and Bax inhibitor-1 (BI-1). The activated IRE1α triggers different downstream pathways depending on the UPRosome formed by distinct modulator proteins. At the initial phase of ER stress, IRE1α-XBP1 axis functions as an adaptive response. While ER stress sustains or intensifies, signals shift to apoptotic responses. Furthermore, IRE1α signaling can be exploited to the development of a wide range of prevalent human diseases, with cancer the most characterized. Here we provide an overview of recent insights into the complex IRE1α signaling network which makes IRE1α an intriguing cell fate switch. Besides, the functional relevance is presented since IRE1α a...Continue Reading

Citations

Mar 25, 2017·Journal of Alzheimer's Disease : JAD·Xin-Jun LiuFeng-Xue Lao
Jan 10, 2018·Wound Repair and Regeneration : Official Publication of the Wound Healing Society [and] the European Tissue Repair Society·Tatiana V BoykoGeorge P Yang
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Mar 23, 2020·Journal of Cell Communication and Signaling·Shekufe Rezghi BarezMahmoud Aghaei
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Feb 11, 2021·Biomedicines·Natalia SiweckaIreneusz Majsterek
Aug 1, 2021·The FEBS Journal·Nataša Pavlović, Femke Heindryckx

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