Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
CY Liu, M Schröder, RJ Kaufman - Journal of Biological Chemistry, 2000 - ASBMB
IRE1 and PERK are type I transmembrane serine/threonine protein kinases that are
activated by unfolded proteins in the endoplasmic reticulum (ER) to signal adaptive
responses. IRE1 is present in all eukaryotic cells and signals the unfolded protein response
through its kinase and endoribonuclease activities. PERK signals phosphorylation of a
translation initiation factor to inhibit protein synthesis in higher eukaryotic cells but is absent
in the Saccharomyces cerevisiae genome. The amino acid sequences of the amino-terminal …
activated by unfolded proteins in the endoplasmic reticulum (ER) to signal adaptive
responses. IRE1 is present in all eukaryotic cells and signals the unfolded protein response
through its kinase and endoribonuclease activities. PERK signals phosphorylation of a
translation initiation factor to inhibit protein synthesis in higher eukaryotic cells but is absent
in the Saccharomyces cerevisiae genome. The amino acid sequences of the amino-terminal …
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