Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2002-1-7
pubmed:abstractText
The unfolded protein response (UPR) is a transcriptional and translational intracellular signaling pathway activated by the accumulation of unfolded proteins in the lumen of the endoplasmic reticulum (ER). We have used C. elegans as a genetic model system to dissect UPR signaling in a multicellular organism. C. elegans requires ire-1-mediated splicing of xbp-1 mRNA for UPR gene transcription and survival upon ER stress. In addition, ire-1/xbp-1 acts with pek-1, a protein kinase that mediates translation attenuation, in complementary pathways that are essential for worm development and survival. We propose that UPR transcriptional activation by ire-1 as well as translational attenuation by pek-1 maintain ER homeostasis. The results demonstrate that the UPR and ER homeostasis are essential for metazoan development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/IRE1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase..., http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/XBP1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
107
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
893-903
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11779465-Animals, pubmed-meshheading:11779465-Caenorhabditis elegans, pubmed-meshheading:11779465-Caenorhabditis elegans Proteins, pubmed-meshheading:11779465-Cell Cycle Proteins, pubmed-meshheading:11779465-Fungal Proteins, pubmed-meshheading:11779465-MAP Kinase Kinase 1, pubmed-meshheading:11779465-Membrane Glycoproteins, pubmed-meshheading:11779465-Mitogen-Activated Protein Kinase Kinases, pubmed-meshheading:11779465-Molecular Sequence Data, pubmed-meshheading:11779465-Mutation, pubmed-meshheading:11779465-Protein Folding, pubmed-meshheading:11779465-Protein-Serine-Threonine Kinases, pubmed-meshheading:11779465-Repressor Proteins, pubmed-meshheading:11779465-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11779465-Signal Transduction, pubmed-meshheading:11779465-Transcription Factors, pubmed-meshheading:11779465-Transcriptional Activation
pubmed:year
2001
pubmed:articleTitle
Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development.
pubmed:affiliation
Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.