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Article

IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA.

Nature - 3 Jan 2002

Calfon Marcella, Zeng Huiqing, Urano Fumihiko, Till Jeffery H, Hubbard Stevan R, Harding Heather P, Clark Scott G, Ron David

Abstract excerpt

The unfolded protein response (UPR), caused by stress, matches the folding capacity of endoplasmic reticulum (ER) to the load of client proteins in the organelle. In yeast, processing of HAC1 mRNA by activated Ire1 leads to synthesis of the transcription factor Hac1 and activation of the UPR. The responses to activated IRE1 in metazoans are less well understood. Here we demonstrate that mutations in either ire-1...

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PMID: 11780124
DOI: 10.1038/415092a

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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An essential role for XBP-1 in host protection against immune activation in C. elegans.Semantic proximity Read ↗

Unfolded protein response transducer IRE1-mediated signaling independent of XBP1 mRNA splicing is not required for growth and development of medaka fishSemantic proximity Read ↗

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