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XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor
The transcription factor XBP1, a target of ATF6, is identified as a mammalian substrate of such an unconventional mRNA splicing system and it is shown that only the spliced form of X BP1 can activate the UPR efficiently. Expand
ATF6 Activated by Proteolysis Binds in the Presence of NF-Y (CBF) Directly to the cis-Acting Element Responsible for the Mammalian Unfolded Protein Response
It is concluded that specific and direct interactions between ATF6 and ERSE are critical for transcriptional induction not only of ER chaperones but also of CHOP and XBP-1. Expand
Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1.
It is demonstrated that ATF6alpha functions as a critical regulator of ER quality control proteins in mammalian cells, in marked contrast to worm and fly cells in which IRE1 is responsible. Expand
Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated Proteins
The results suggest that, as in yeast, bZIP proteins are involved in mammalian UPR, acting through newly defined ERSE,acting through newlydefined ERSE. Expand
IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response.
It is proposed that nuclear- localized IRE1alpha and cytoplasmic-localized ATF6 signaling pathways merge through regulation of XBP1 activity to induce downstream gene expression. Expand
Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins
This work provides new insight into how a stress response pathway can be structured to allow cells to avert death as they adapt and underscores the contribution of posttranscriptional and posttranslational mechanisms in influencing this outcome. Expand
A time-dependent phase shift in the mammalian unfolded protein response.
It is shown here that degradation of misfolded glycoprotein substrates requires transcriptional induction of EDEM (ER degradation-enhancing alpha-mannosidase-like protein), and that this is mediated specifically by IRE1-XBP1 and not by ATF6. Expand
Refinement of odor molecule tuning by dendrodendritic synaptic inhibition in the olfactory bulb.
The mechanism of olfactory discrimination by single unit recordings of responses to a series of normal aliphatic aldehydes from individual rabbit M/T cells was investigated and revealed that inhibitory responses are evoked in a M/ T cell by a defined subset of odor molecules with structures closely related to the excitatory odor molecules. Expand
Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum
  • K. Mori
  • Biology, Medicine
  • Cell
  • 26 May 2000
The cellular responses to the accumulation of unfolded proteins in the ER are much more extensive than previously recognized and will provide new insights into not only fundamental principles in cell biology but also the pathogenesis of diseases that result from problems in protein folding in theER. Expand
AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1.
It is proved that TRX can associate directly with Ref-1 in the nucleus and the requirement of cysteine residues in the TRX catalytic center for the potentiation of AP-1 activity is demonstrated. Expand