Article Abstract:
Endoribonuclease activity of IRE1 in mammals has been found to autoregulate its mRNA and to be necessary for the unfolded protein response (UPR). IRE1(beta) single-amino acid substitution mutants were used to show that the RNase activity is necessary for UPR activation by IRE1(alpha) and IRE1(beta). The study also used in vitro cleavage assays and functional analyses.
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Article Abstract:
In response to unfolded protein in the endoplasmic reticulum (ER) eukaryotes regulate the transcription of genes encoding ER protein chaperones upward. A novel human cDNA encoding a homolog to Saccharomyces cerevisiae Ire1p has been isolated. Ire1p is a proximal sensor for the signal transduction pathway in yeast. A stress-response path from the ER to the nucleus must have a novel bifunctional protein kinase/endoribonuclease (Ire1p) in cells of mammals.
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Article Abstract:
Stress signaling of the lumen of the endoplasmic reticulum (ER), which is a protein-folding compartment, involves coordination of gene translation and transcription regulation. The lumen sends diverse signals, including protein kinases that respond to unfolded protein in the ER. The Saccharomyces cerevisiae unfolded protein response (UPR), the proximal sensor for he UPR, Ire1P, Hac1p, a basic leucine zipper transcription factor activating yeast UPR, mammalian UPR and UPR element (UPRE), apoptosis, and other topics are discussed and the current body of knowledge is reviewed.
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