Regulation of the early stages of endoplasmic reticulum inheritance during ER stress

Chao, Jesse T.; Piña, Francisco; Niwa, Maho

doi:10.1091/mbc.e20-08-0558

Cited by 7 publications

(3 citation statements)

References 44 publications

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“…Research on the involvement of Slt2 in UPR(46,60,70) have primarily focused on the slt2Δ cell grown in the presence of ER stressors for a short duration (one hour). For instance, Chen at al.…”

Section: Discussionmentioning

confidence: 99%

“…One potential scenario involves a specific signaling input originating from the Slt2 pathway, achieved through the phosphorylation of one of its reported substrates. This phosphorylated substrate may collaborate with the Hac1 to activate a particular physiological response.Research on the involvement of Slt2 in UPR(46,60,70) have primarily focused on the slt2Δ cell grown in the presence of ER stressors for a short duration (one hour). For instance, Chen at al.…”

mentioning

confidence: 99%

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Adaptation to ER Stress by Slt2, Counterpart of Human MAP Kinase ERK1/2, via Enhancing Splicing and Translation ofHAC1mRNA inSaccharomyces cerevisiae

Uppala,

Chakraborty,

George

et al. 2023

Preprint

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Unfolded protein response (UPR) is a cellular strategy to increase the protein folding capacity of cells in response to stress within the endoplasmic reticulum (ER). In metazoan cells, three major UPR sensors Ire1, PERK and ATF6 work in concert by simultaneously activating intracellular signaling pathways and modulating a series of physiological processes such as attenuation of the general protein synthesis and expression of protein chaperones. In yeastSaccharomyces cerevisiae, Ire1 is known to be the only UPR sensor, which mediates splicing ofHAC1mRNA in the cytoplasm and derepresses its translation. Hac1 is a transcription factor that increases the expression of protein folding enzymes and chaperones, thus enhancing the protein folding capacity of cells. In this study, we provide compelling evidence that kinase Slt2 plays a significant role in facilitating both the splicing and translation ofHAC1mRNA, while also serving as a key mediator in the activation of UPR genes through an alternative route. We also provide evidence that human extracellular signal-regulated kinase 1 (ERK1) or ERK2 served as a functional substitute for yeast Slt2 in the context of UPR. Furthermore, ERK1 exhibits an enhanced activation in human primary cells when grown in the presence of ER stressor. These findings collectively suggest that Slt2 responds to ER stress by activating the Ire1 pathway as well as initiating a parallel signaling pathway.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Adaptation to ER Stress by Slt2, Counterpart of Human MAP Kinase ERK1/2, via Enhancing Splicing and Translation ofHAC1mRNA inSaccharomyces cerevisiae

Uppala,

Chakraborty,

George

et al. 2023

Preprint

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“…Cells are highly dynamic in life processes, and their functions are constantly under the regulation of a set of intracellular organelles . Among the various organelles in eukaryotic cells, the endoplasmic reticulum (ER) is the largest cytoplasmic membrane structure that carries a series of important biological macromolecules and plays a crucial role in many significant physiological processes, such as lipid synthesis, intracellular Ca 2+ signal transduction, and protein synthesis, folding, and posttranslational modification . Factors such as hypoxia, starvation, and oxidative stress can lead to the accumulation of unfolded or misfolded proteins in the ER lumen, causing ER stress to activate the unfolded protein response (UPR) .…”

mentioning

confidence: 99%

Dynamic Visualization of Endoplasmic Reticulum Stress in Living Cells via a Two-Stage Cascade Recognition Process

Zhou

Wang

et al. 2022

Anal. Chem.

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The endoplasmic reticulum (ER) is crucial for the regulation of multiple cellular processes, such as cellular responses to stress and protein synthesis, folding, and posttranslational modification. Nevertheless, monitoring ER physiological activity remains challenging due to the lack of powerful detection methods. Herein, we built a two-stage cascade recognition process to achieve dynamic visualization of ER stress in living cells based on a fluorescent carbon dot (CD) probe, which is synthesized by a facile one-pot hydrothermal method without additional modification. The fluorescent CD probe enables two-stage cascade ER recognition by first accumulating in the ER as the positively charged and lipophilic surface of the CD probe allows its fast crossing of multiple membrane barriers. Next, the CD probe can specifically anchor on the ER membrane via recognition between boronic acids and o-dihydroxy groups of mannose in the ER lumen. The two-stage cascade recognition process significantly increases the ER affinity of the CD probe, thus allowing the following evaluation of ER stress by tracking autophagy-induced mannose transfer from the ER to the cytoplasm. Thus, the boronic acid-functionalized cationic CD probe represents an attractive tool for targeted ER imaging and dynamic tracking of ER stress in living cells.

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Regulation of the early stages of endoplasmic reticulum inheritance during ER stress

Cited by 7 publications

References 44 publications

Adaptation to ER Stress by Slt2, Counterpart of Human MAP Kinase ERK1/2, via Enhancing Splicing and Translation ofHAC1mRNA inSaccharomyces cerevisiae

Adaptation to ER Stress by Slt2, Counterpart of Human MAP Kinase ERK1/2, via Enhancing Splicing and Translation ofHAC1mRNA inSaccharomyces cerevisiae

Dynamic Visualization of Endoplasmic Reticulum Stress in Living Cells via a Two-Stage Cascade Recognition Process

Reticulons bind sphingolipids to activate the endoplasmic reticulum cell cycle checkpoint, the ER surveillance pathway

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