ER homeostasis and autophagy

Smith, Matthew D.; Wilkinson, Simon

doi:10.1042/ebc20170092

Cited by 176 publications

(136 citation statements)

References 79 publications

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“…). Importantly, ER‐phagy responses – also termed reticulophagies ‐ and related processes are emerging as mechanistically diverse and important players in ER remodelling; ER‐phagy has been observed in insect , plant , yeast and mammalian cells . This review will also demonstrate that such ER‐phagy also plays a key role in normal physiology and may be overwhelmed or aberrant in a number of disease conditions, including neurodegenerative disorders or cancer.…”

Section: Introductionmentioning

confidence: 90%

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ER‐phagy: shaping up and destressing the endoplasmic reticulum

2019

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The endoplasmic reticulum (ER) network has central roles in metabolism and cellular organization. The ER undergoes dynamic alterations in morphology, molecular composition and functional specification. Remodelling of the network under fluctuating conditions enables the continual performance of ER functions and minimizes stress. Recent data have revealed that selective autophagy‐mediated degradation of ER fragments, or ER‐phagy, fundamentally contributes to this remodelling. This review provides a perspective on established views of selective autophagy, comparing these with emerging mechanisms of ER‐phagy and related processes. The text discusses the impact of ER‐phagy on the function of the ER‐ and the cell, both in normal physiology and when dysregulated within disease settings. Finally, unanswered questions regarding the mechanisms and significance of ER‐phagy are highlighted.

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Section: Introductionmentioning

confidence: 90%

“…Recent findings have revealed that autophagy, the transport of cytoplasmic components into the lysosome for degradation, is a key ER remodelling process . Two main forms of autophagy regulate ER status.…”

Section: Introductionmentioning

confidence: 99%

ER‐phagy: shaping up and destressing the endoplasmic reticulum

2019

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“…The endoplasmic reticulum (ER) is an organelle where proteins and lipids are synthesized and modified and serves as a calcium reservoir. The ER is also a site where the unfolded protein response (UPR) or ER UPR occurs (Smith & Wilkinson, ). When misfolded proteins accumulate under various stress conditions, the ER UPR is activated to degrade the misfolded proteins through three key pathways including the protein kinase RNA‐like ER kinase (PERK), the inositol‐requiring enzyme‐1 (IRE‐1)/X‐box binding protein‐1 (XBP‐1), and the activating transcription factor 6 (ATF6) pathways.…”

Section: Age‐dependent Changesmentioning

confidence: 99%

Age‐dependent changes and biomarkers of aging in Caenorhabditis elegans

et al. 2019

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Caenorhabditis elegans is an exceptionally valuable model for aging research because of many advantages, including its genetic tractability, short lifespan, and clear age‐dependent physiological changes. Aged C. elegans display a decline in their anatomical and functional features, including tissue integrity, motility, learning and memory, and immunity. Caenorhabditis elegans also exhibit many age‐associated changes in the expression of microRNAs and stress‐responsive genes and in RNA and protein quality control systems. Many of these age‐associated changes provide information on the health of the animals and serve as valuable biomarkers for aging research. Here, we review the age‐dependent changes in C. elegans and their utility as aging biomarkers indicative of the physiological status of aging.

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“…ER stress can be induced in response to many cellular perturbations, such as oxidative stress, in turn activating an evolutionary conserved signaling pathway named the unfolded protein response (UPR) [3][4][5]. The main aim of UPR is to counteract ER stress through the inhibition of protein translation, enhancing its ability for protein folding and accelerating protein degradation, and to restore ER homeostasis [4,6,7]. However, the excessive or persistent induction of the UPR may change its initial function from adaptation to cell death induction, which has been shown to contribute to the pathogenesis of various diseases, including liver diseases [8].…”

Section: Introductionmentioning

confidence: 99%

Activation of the IRE1α Arm, but not the PERK Arm, of the Unfolded Protein Response Contributes to Fumonisin B1-Induced Hepatotoxicity

Liu

Zhang

Yin

et al. 2020

Toxins

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Previous studies by us or others have shown that endoplasmic reticulum (ER) stress was activated by fumonisin 1 (FB1) exposure, which is considered to be a critical event in the FB1-induced toxic effect. However, the detailed mechanisms underlying FB1-induced ER stress-mediated liver toxicity remain elusive. The objectives of the present study were designed to address the following issues: (1) the contribution of each arm of the unfolded protein response (UPR); (2) the downstream targets of ER stress that mediated FB1-induced liver toxicity; and (3) the relationship between ER stress and oxidative stress triggered by FB1. We also investigated whether the inhibition of ER stress by its inhibitor could offer protection against FB1-induced hepatotoxicity in vivo, which has not been critically addressed previously. The results showed that the activation of the IRE1α axis, but not of the PERK axis, of UPR contributed to FB1-induced ER stress-mediated hepatocyte toxicity; the activation of the Bax/Bak-mediated mitochondrial pathway lay downstream of IRE1α to trigger mitochondrial-dependent apoptosis in response to FB1; FB1-induced oxidative stress and ER stress augmented each other through a positive feedback mechanism; tauroursodeoxycholic acid (TUDCA)-mediated ER stress inactivation is an effective approach to counteract FB1-induced hepatotoxicity in vivo. The data of the present study allow us to better understand the mechanisms of FB1-induced hepatotoxicity.

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ER homeostasis and autophagy

Cited by 176 publications

References 79 publications

ER‐phagy: shaping up and destressing the endoplasmic reticulum

ER‐phagy: shaping up and destressing the endoplasmic reticulum

Age‐dependent changes and biomarkers of aging in Caenorhabditis elegans

Activation of the IRE1α Arm, but not the PERK Arm, of the Unfolded Protein Response Contributes to Fumonisin B1-Induced Hepatotoxicity

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