About: An unfolded protein-induced conformational switch activates mammalian IRE1

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About: An unfolded protein-induced conformational switch activates mammalian IRE1 Goto Sponge NotDistinct Permalink

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	An unfolded protein-induced conformational switch activates mammalian IRE1
Creator	Walter, Peter Acosta-Alvear, Diego Chu, Feixia Kay, Lewis Lee, Crystal Nguyen, Hieu Elif Karagö Z, G
Source	Medline; PMC
abstract	The unfolded protein response (UPR) adjusts the cell’s protein folding capacity in the endoplasmic reticulum (ER) according to need. IRE1 is the most conserved UPR sensor in eukaryotic cells. It has remained controversial, however, whether mammalian and yeast IRE1 use a common mechanism for ER stress sensing. Here, we show that similar to yeast, human IRE1α’s ER-lumenal domain (hIRE1α LD) binds peptides with a characteristic amino acid bias. Peptides and unfolded proteins bind to hIRE1α LD’s MHC-like groove and induce allosteric changes that lead to its oligomerization. Mutation of a hydrophobic patch at the oligomerization interface decoupled peptide binding to hIRE1α LD from its oligomerization, yet retained peptide-induced allosteric coupling within the domain. Importantly, impairing oligomerization of hIRE1α LD abolished IRE1’s activity in living cells. Our results provide evidence for a unifying mechanism of IRE1 activation that relies on unfolded protein binding-induced oligomerization.
has issue date	2017-10-03(xsd:dateTime)
bibo:doi	10.7554/elife.30700
bibo:pmid	28971800
has license	cc-by
sha1sum (hex)	79233a0dcabd313110b3256113778d814f7bc902
schema:url	https://doi.org/10.7554/elife.30700
resource representing a document's title	An unfolded protein-induced conformational switch activates mammalian IRE1
has PubMed Central identifier	PMC5699868
has PubMed identifier	28971800
schema:publication	eLife
resource representing a document's body	covid:79233a0dcabd313110b3256113778d814f7bc902#body_text
is schema:about of	named entity 'PEPTIDE BINDING' named entity 'ITS' named entity 'IRE1 ACTIVATION' named entity '27S' named entity 'EUKARYOTIC CELLS' named entity 'LEAD' named entity 'ER STRESS' named entity 'OUR' named entity 'NEED' named entity 'HERE' named entity 'INTERFACE' named entity 'SIMILAR' named entity 'COUPLING' named entity 'UNFOLDED' named entity 'ACTIVITY' named entity 'unfolded protein response' named entity 'oligomerization' named entity 'IRE1' named entity 'peptides' named entity 'capacity' named entity 'yeast' named entity 'allosteric' named entity 'unfolded' named entity 'SWITCH' named entity 'MUTATION' named entity 'IMPAIRING' named entity 'GROOVE' named entity 'BIND' named entity 'ACCORDING' named entity 'PROVIDE' named entity 'MHC' named entity 'AMINO ACID' named entity 'USE' named entity 'EVIDENCE FOR' named entity 'UNFOLDED PROTEIN RESPONSE' named entity 'MECHANISM' named entity 'PEPTIDE' named entity 'THE CELL' named entity 'ACTIVATES' named entity 'INDUCED' named entity 'IRE1' named entity 'MAMMALIAN' named entity 'OLIGOMERIZATION' named entity 'DOMAIN' named entity 'BINDS' named entity 'CELLS' named entity 'CONSERVED' named entity 'CAPACITY' named entity 'CHANGES' named entity 'A COMMON' named entity 'PROTEINS' named entity 'ENDOPLASMIC RETICULUM' named entity 'HUMAN' named entity 'ABOLISHED' named entity 'RESULTS' named entity 'INDUCE' named entity 'MAMMALIAN' named entity 'SENSING' named entity 'IRE1A' named entity 'YEAST' named entity 'ER-' named entity 'LIVING' named entity 'IRE1' named entity 'UNFOLDED PROTEIN' named entity 'SENSOR' named entity 'LIKE' named entity 'CHARACTERISTIC' named entity 'INDUCED' named entity 'HYDROPHOBIC' named entity 'PROTEIN FOLDING' named entity 'PATCH' named entity 'BIAS' named entity 'RETAINED' named entity 'PEPTIDES' named entity 'UNFOLDED PROTEIN BINDING'

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