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. 1996 Nov 1;87(3):391-404.
doi: 10.1016/s0092-8674(00)81360-4.

A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

J S Cox  1 , P Walter
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Free article

A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

J S Cox et al. Cell. .
Free article

Abstract

Cells respond to an accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing transcription of genes encoding ER-resident proteins. The information is transmitted from the ER lumen to the nucleus by an intracellular signaling pathway, the unfolded protein response (UPR). We have identified a basic-leucine zipper transcription factor, Hac1p, that is required for the UPR and binds to the UPR element in the promoter of UPR-regulated genes. Surprisingly, Hac1p is found in UPR-activated cells only, and its level is controlled by regulated splicing of its mRNA. Splicing replaces the C-terminal tail of Hac1p with a different peptide that renders Hac1p more resistant to an otherwise extremely rapid ubiquitin-dependent degradation. We propose that the complex regulation of Hac1p expression serves to provide multiple levels at which the UPR can be controlled.

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Comment in

  • Mixed mechanisms in yeast pre-mRNA splicing?
    Rosbash M. Rosbash M. Cell. 1996 Nov 1;87(3):357-9. doi: 10.1016/s0092-8674(00)81355-0. Cell. 1996. PMID: 8898188 Review. No abstract available.
  • An elegant UPR discovery.
    Taylor RC. Taylor RC. Nat Rev Mol Cell Biol. 2018 Sep;19(9):545. doi: 10.1038/s41580-018-0043-9. Nat Rev Mol Cell Biol. 2018. PMID: 30030525 No abstract available.

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