The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway
نویسندگان
چکیده
منابع مشابه
The unfolded-protein-response pathway in yeast.
The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the increased production of several ER-resident proteins. This signalling pathway exists in organisms as divergent as mammals and yeast, and is the only known example of an intracellular signalling system that links the ER and the nucleus. Recently, a transmembrane kinase similar in structure to growth-factor recep...
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The protein folding capabilities in the endoplasmic reticulum (ER) are disturbed by alternations in the cellular homeostasis such as the disruption of calcium ion homeostasis, the expression of mutated proteins and oxidative stress. In response to these ER dysfunctions, eukaryotic cells activate canonical branches of signal transduction cascades to restore the protein folding capacity and avoid...
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The unfolded protein response (UPR) is a stress response conserved in eukaryotic organisms and activated by the accumulation of misfolded proteins in the endoplasmic reticulum (ER). Adverse environmental conditions disrupt protein folding in the ER and trigger the UPR. Recently, it was found that the UPR can be elicited in the course of plant development and defense. During vegetative plant dev...
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Endoplasmic reticulum (ER) stress induces the unfolded protein response (UPR), an essential adaptive intracellular pathway that relieves the stress. Although the UPR is an evolutionarily conserved and beneficial pathway, its chronic activation contributes to the pathogenesis of a wide variety of human disorders. The fidelity of UPR activation must thus be tightly regulated to prevent inappropri...
متن کاملThe unfolded protein response: from stress pathway to homeostatic regulation.
The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled proteins advance from the ER to the cell surface. To ascertain fidelity in protein folding, cells regulate the protein-folding capacity in the ER according to need. The ER responds to the burden of unfolded proteins in it...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2011
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1117184109