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The accumulation of unfolded proteins within the endoplasmic recticulum (ER) of yeast and mammalian cells activates the unfolded protein response (UPR) pathway and leads to the transcription of ER-specific genes involved in protein folding. The activation of the UPR requires the ER transmembrane kinase IRE1p (for inositol-requiring and ER-to-nucleus signaling protein). IRE1alpha and IRE1beta are two mammalian homologs of the yeast IRE1p. These related proteins localize to the ER lumen and contain both a short transmembrane domain that spans the ER membrane and a cytosolic Ser/Thr kinase domain. IRE1 activation involves the oligomerization and trans-phosphorylation of the cytosolic portion of the proteins, which then potentiates its intrinsic kinase activity and, in turn, stimulates transcription of UPR-targeted genes. Protein function: Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins. [The UniProt Consortium]
This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the usability of this website, serve for direct advertising or simplify interaction with other websites and social networks, will only be used with your consent.
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