![]() Academic, pp 79–125Ĭalfon M, Zeng H, Urano F et al (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. In: Progress in nucleic acid research and molecular biology. Genetics 77:71–94īrostrom CO, Brostrom MA (1997) Regulation of translational initiation during cellular responses to stress. īrenner S (1974) The genetics of Caenorhabditis elegans. īlackwell TK, Steinbaugh MJ, Hourihan JM et al (2015) SKN-1/Nrf, stress responses, and aging in Caenorhabditis elegans. īar-Ziv R, Frakes AE, Higuchi-Sanabria R et al (2020) Measurements of physiological stress responses in C. Īgani F, Jiang B-H (2013) Oxygen-independent regulation of HIF-1: novel involvement of PI3K/AKT/mTOR pathway in cancer. Nascent polypeptide-associated complex NMD:Īballay A, Ausubel FM (2001) Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from salmonella typhimurium-mediated killing. KeywordsĪrsenic-inducible proteasomal 19S regulatory particle-associated protein COPII:ĮR-associated proteasomal degradation ERES: Caenorhabditis elegans model system has critically contributed to these unprecedented aspects of the ER UPR and broadens the possible therapeutic targets to treat the ER-stress associated human disorders and time-dependent physiological deterioration of aging. Recent development in the research of the UPR includes cell-nonautonomous features of the UPR, interplay between the UPR and other stress response pathways, unconventional UPR inducers, and noncanonical UPR independent of the three major branches, originated from multiple cellular and molecular machineries in addition to ER. Therefore, the effective UPR to internal and external causes is linked to the multiple pathophysiological conditions such as aging, immunity, and neurodegenerative diseases. The integrated responses act on to resolve the ER stress by increasing protein folding capacity, attenuating ER-loading translation, activating ER-associated proteasomal degradation (ERAD), and regulating IRE1-dependent decay of mRNA (RIDD). In metazoan, the UPR pathways consisted of IRE1/XBP1, PEK-1 and ATF6, which function in parallel and downstream transcriptional activation triggers the proteostasis networks consisting of molecular chaperones, protein degradation machinery and other stress response pathways ((Labbadia J, Morimoto RI, F1000Prime Rep 6:7, 2014) (Shen X, Ellis RE, Lee K, Annu Rev Biochem 28:893-903, 2014)). Physiological demands, environmental perturbations and pathological conditions can cause accumulation of unfolded proteins in the ER and the stress signal is transmitted to the nucleus to turn on a series of genes to respond the challenge. The unfolded protein response (UPR) is an evolutionarily conserved adaptive regulatory pathway that alleviates protein-folding defects in the endoplasmic reticulum (ER).
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