Endoplasmic reticulum stress responses

By M. Schröder. Cellular and Molecular Life Sciences, 2008

686 citations recorded by the source corpus.

Abstract.In homeostasis, cellular processes are in a dynamic equilibrium. Perturbation of homeostasis causes stress. In this review I summarize how perturbation of three major functions of the endoplasmic reticulum (ER) in eukaryotic cells–protein folding, lipid and sterol biosynthesis, and storing intracellular Ca2+ – causes ER stress and activates signaling pathways collectively termed the unfolded protein response (UPR). I discuss how the UPR reestablishes homeostasis, and summarize our current understanding of how the transition from protective to apoptotic UPR signaling is controlled, and how the UPR induces inflammatory signaling.

Subfields: Cell Biology, Epidemiology, Surgery

View Paper: https://www.semanticscholar.org/paper/21690b6b5ce865aaa4d0194c78215d81dd4c62e0

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In Cell Biology

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Citations in the corpus

• Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. (2011, background): “The UPR includes upregulation of ER-located chaperones to assist folding of aggregationprone proteins; a selective inhibition of overall protein synthesis to reduce the ER work load, while selectively favoring synthesis of proteins that augment the UPR; and transport of misfolded proteins to the ubi”
• Immunogenic cell death and DAMPs in cancer therapy (2012, background): “These authors showed that a recombinant N-terminal fragment of CRT (39-272) is a potent inducer of activation and maturation of B cells and macrophages and can trigger Ig class switching in B cells without T cell help in vitro and in vivo72.”
• Oxidative stress in ALS: key role in motor neuron injury and therapeutic target. (2010, background): “ER chaperones such as BiP help to refold these proteins or expel them through the ER-associated protein degradation (ERAD) pathway, misfolded proteins tend to accumulate within the ER, leading to ER stress [127].”