The unfolded protein response in nutrient sensing and differentiation
By R. Kaufman, D. Scheuner, M. Schröder, Xiaohua Shen, Kyungho Lee, Chuan-Yin Liu, Stacey M. Arnold. Nature reviews. Molecular cell biology, 2002
664 citations recorded by the source corpus.
Eukaryotic cells coordinate protein-folding reactions in the endoplasmic reticulum with gene expression in the nucleus and messenger RNA translation in the cytoplasm. As the rate of protein synthesis increases, protein folding can be compromised, so cells have evolved signal-transduction pathways that control transcription and translation — the 'unfolded protein response'. Recent studies indicate that these pathways also coordinate rates of protein synthesis with nutrient and energy stores, and regulate cell differentiation to survive nutrient-limiting conditions or to produce large amounts of secreted products such as hormones, antibodies or growth factors.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/20ad2a8c014906e026ad0c4b7e663702dbef2792
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Citations in the corpus
- Growth Arrest and DNA Damage-Inducible Protein GADD34 Targets Protein Phosphatase 1α to the Endoplasmic Reticulum and Promotes Dephosphorylation of the α Subunit of Eukaryotic Translation Initiation Factor 2 (2003, methodology): “The ability of WT GADD34(1-674) but not GADD34(1-600) to bind PP1 in the coimmunoprecipitation and affinity isolation assays suggested that the C terminus of GADD34 between amino acids 600 to 674 was crucial for PP1 binding.”
- Orchestrating the unfolded protein response in health and disease. (2002, background): “Because proteins have different ATP requirements for protein folding prior to export, it has been proposed that the threshold for UPR activation might differ among various cell types, depending on their energy stores and the amount and nature of the secretory proteins they produce (4).”
- Translational control in stress and apoptosis (2005, background): “It was proposed that blood glucose levels could influence the folding status of proteins in the ER and signal, through PERK and eIF2α, to cause a reduction in protein synthesi”
- Phosphorylation of the α Subunit of Eukaryotic Initiation Factor 2 Is Required for Activation of NF-κB in Response to Diverse Cellular Stresses (2003, background): “ER chaperones GRP78/BiP and GRP94 (22, 35, 47).”
- The impact of the unfolded protein response on human disease (2012, background): “This result suggests that IRE1 may play a more significant role in ER expansion associated with differentiation of secretory cell types than with the adaptation to ER stress (Kaufman et al., 2002; Cross et al., 2012).”
- Protein carbonylation, cellular dysfunction, and disease progression (2006, background): “This qualitycontrol mechanism, involving a remarkable series of glycosylation/deglycosylation reactions, enables correctly folded proteins to be distinguished from misfolded ones: incorrectly folded proteins are detected by the quality-control mechanism and sent along another pathway (the "unfolded ”
- Coupling endoplasmic reticulum stress to the cell death program (2004, background): “damaged, dysfunctional cells but also as part of a recycling mechanism to allow recovery of organ function.(3,4,7)”
- Translational control in the endoplasmic reticulum stress response. (2002, background): “It is possible, however, that the special glucose transport properties of β cells cause PERK to be activated at physiologically low glucose levels (29).”
- Principles of protein folding, misfolding and aggregation. (2004, background): “[42] Kaufman RJ, Scheuner D, Schroder M, Shen X, Lee K, Liu CY,”