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IRE1 Initiates XBP-1 Independent Pathway for mRNA Degradation in Unfolded Protein Response

This study explores the role of IRE1 in the unfolded protein response (UPR) and its ability to initiate an XBP-1 independent pathway. Findings reveal that IRE1's nuclease activity targets a broader range of mRNA substrates compared to XBP-1, facilitating the rapid degradation of specific mRNAs. This degradation process relies on endoplasmic reticulum (ER) localization and the peptide sequence. Importantly, mRNA repression by IRE1 is attributed to stability rather than transcriptional inhibition, and cleavage of mRNA is essential for its decay, which requires cotranslational processes.

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IRE1 Initiates XBP-1 Independent Pathway for mRNA Degradation in Unfolded Protein Response

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  1. Major Claims • IRE1 initiates an XBP-1 independent pathway during the unfolding protein response • IRE1 nuclease has a broader range of substrates than XBP-1 • IRE1 mediates the rapid degradation of a subset of mRNA • Degradation is dependent on ER localization and peptide sequence

  2. No treatment Actinomycin D Treat with DTT Treat with both

  3. 3’ fragment 5’ fragment

  4. Conclusions • IRE1 mediates repression of ER targeted mRNA • Repression is due to mRNA stability not transcription • Cleavage of mRNA initiates degradation • mRNA decay requires cotranslational translocation and translation of the correct peptide

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