Open Close
Reference
Citation
Hollien, J., Weissman, J.S. (2006). Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response.  Science 313(5783): 104--107.
FlyBase ID
FBrf0192887
Publication Type
Research paper
Abstract

The unfolded protein response (UPR) allows the endoplasmic reticulum (ER) to recover from the accumulation of misfolded proteins, in part by increasing its folding capacity. Inositol-requiring enzyme-1 (IRE1) promotes this remodeling by detecting misfolded ER proteins and activating a transcription factor, X-box-binding protein 1, through endonucleolytic cleavage of its messenger RNA (mRNA). Here, we report that IRE1 independently mediates the rapid degradation of a specific subset of mRNAs, based both on their localization to the ER membrane and on the amino acid sequence they encode. This response is well suited to complement other UPR mechanisms because it could selectively halt production of proteins that challenge the ER and clear the translocation and folding machinery for the subsequent remodeling process.

PubMed ID
PubMed Central ID
Related Publication(s)
Supplementary material
Note

Cell biology. Stressed cells cope with protein overload.
Ron, 2006, Science 313(5783): 52--53 [FBrf0195144]

Associated Information
Comments
Associated Files
Other Information
Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Science
    Title
    Science
    Publication Year
    1895-
    ISBN/ISSN
    0036-8075
    Data From Reference