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Trends Biochem Sci. 2014 May;39(5):245-54. doi: 10.1016/j.tibs.2014.02.008. Epub 2014 Mar 20.

Getting RIDD of RNA: IRE1 in cell fate regulation.

Author information

1
Department of Medical Protein Research, VIB, Ghent, Belgium; Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium. Electronic address: m.marionmaurel@gmail.com.
2
INSERM U1053, Université Bordeaux Segalen, 33000 Bordeaux, France; Centre Régional de Lutte Contre le Cancer Eugène Marquis, 35000 Rennes, France.
3
Department of Medical Protein Research, VIB, Ghent, Belgium; Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
4
Department of Medical Protein Research, VIB, Ghent, Belgium; Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium. Electronic address: sarah.gerlo@vib-ugent.be.

Abstract

Inositol-requiring enzyme 1 (IRE1) is the most conserved transducer of the unfolded protein response (UPR), a homeostatic response that preserves proteostasis. Intriguingly, via its endoribonuclease activity, IRE1 produces either adaptive or death signals. This occurs through both unconventional splicing of XBP1 mRNA and regulated IRE1-dependent decay of mRNA (RIDD). Whereas XBP1 mRNA splicing is cytoprotective in response to endoplasmic reticulum (ER) stress, RIDD has revealed many unexpected features. For instance, RIDD cleaves RNA at an XBP1-like consensus site but with an activity divergent from XBP1 mRNA splicing and can either preserve ER homeostasis or induce cell death. Here we review recent findings on RIDD and propose a model of how IRE1 RNase activity might control cell fate decisions.

KEYWORDS:

IRE1; RIDD; RNase; endoplasmic reticulum stress; unfolded protein response

PMID:
24657016
DOI:
10.1016/j.tibs.2014.02.008
[Indexed for MEDLINE]
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