About: Regulated Ire1-dependent decay of messenger RNAs in mammalian cells

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
Creator	Li, Han Hollien, Julie Stevens, Nicole Walter, Peter Lin, Jonathan Weissman, Jonathan
Source	PMC
abstract	Maintenance of endoplasmic reticulum (ER) function is achieved in part through Ire1 (inositol-requiring enzyme 1), a transmembrane protein activated by protein misfolding in the ER. The cytoplasmic nuclease domain of Ire1 cleaves the messenger RNA (mRNA) encoding XBP-1 (X-box–binding protein 1), enabling splicing and production of this active transcription factor. We recently showed that Ire1 activation independently induces the rapid turnover of mRNAs encoding membrane and secreted proteins in Drosophila melanogaster cells through a pathway we call regulated Ire1-dependent decay (RIDD). In this study, we show that mouse fibroblasts expressing wild-type Ire1 but not an Ire1 variant lacking nuclease activity also degrade mRNAs in response to ER stress. Using a second variant of Ire1 that is activated by a small adenosine triphosphate analogue, we show that although XBP-1 splicing can be artificially induced in the absence of ER stress, RIDD appears to require both Ire1 activity and ER stress. Our data suggest that cells use a multitiered mechanism by which different conditions in the ER lead to distinct outputs from Ire1.
has issue date	2009-08-10(xsd:dateTime)
bibo:doi	10.1083/jcb.200903014
bibo:pmid	19651891
has license	cc-by-nc-sa
sha1sum (hex)	5322d3b9f5ee17d5b931f0c32173125d6a7304ed
schema:url	https://doi.org/10.1083/jcb.200903014
resource representing a document's title	Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
has PubMed Central identifier	PMC2728407
has PubMed identifier	19651891
schema:publication	J Cell Biol
resource representing a document's body	covid:5322d3b9f5ee17d5b931f0c32173125d6a7304ed#body_text
is schema:about of	named entity 'IRE1' named entity 'RECOMBINATION' named entity 'ABBREVIATIONS' named entity 'BINDING PROTEIN' named entity 'MEF' named entity 'target' named entity 'Abbreviations' named entity 'REGULATED' named entity 'MAMMALIAN' named entity 'TARGET' named entity 'QPCR' named entity 'MESSENGER' named entity 'DECAY' named entity 'DEPENDENT' named entity 'DECAY' named entity 'FRT' named entity 'UPR' named entity 'MOUSE EMBRYONIC FIBROBLAST' named entity 'DEPENDENT' named entity 'IMMUNOGLOBIN' named entity 'UNFOLDED PROTEIN RESPONSE' named entity 'RNAS' named entity 'CELLS' named entity 'TUNICAMYCIN' named entity 'PROTEIN ' named entity 'IRE1' named entity 'PAPER' named entity 'BIP' named entity 'HUMAN' named entity 'USED' named entity 'REGULATED' named entity 'fibroblast' named entity 'recombination' named entity 'unfolded protein response' named entity 'XBP-1' named entity 'NaCl' named entity 'oligomerization' named entity '3T3' named entity 'gene' named entity 'active site' named entity 'ferritin' named entity 'protein expression' named entity 'RNAi' named entity 'protein' named entity 'quantitative real-time PCR' named entity 'immunoglobin' named entity 'Ire1' named entity 'mRNA' named entity 'SDS' named entity 'mRNA' named entity 'Ire1' named entity 'transcription factor' named entity 'protein' named entity 'Ire1' named entity 'UPR' named entity 'down-regulated' named entity 'cytosolic' named entity 'hybridized' named entity 'glyceraldehyde 3-phosphate dehydrogenase' named entity 'nuclease' named entity 'RNAs' named entity 'stress conditions' named entity 'XBP-1' named entity 'Drosophila melanogaster' named entity 'membrane-spanning' named entity 'mRNAs' named entity 'transgene' named entity 'wild-type' named entity 'mRNA' named entity 'peripheral membrane' named entity 'Ire1' named entity 'protein production' named entity 'polyclonal' named entity 'Ire1' named entity 'DTT' named entity 'Agilent Technologies'

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