Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-4-15
pubmed:abstractText
Upon endoplasmic reticulum (ER) stress, ER-located transmembrane stress sensors evoke diverse protective responses. Although ER stress-dependent activation of the sensor proteins is partly explained through their negative regulation by the ER-located chaperone BiP under non-stress conditions, each of the sensors is also regulated by distinct mechanism(s). For instance, yeast Ire1 is fully activated via its direct interaction with unfolded proteins accumulated in the ER. This insight is consistent with a classical notion that unfolded proteins per se trigger ER-stress responses, while various stress stimuli also seem to activate individual sensors independently of unfolded proteins and in a stimuli-specific manner. These properties may account for the different responses observed under different conditions in mammalian cells, which carry multiple ER-stress sensors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1879-0410
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
135-42
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells.
pubmed:affiliation
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't