|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6716
|
|
pubmed:dateCreated |
1999-2-18
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Protein synthesis and the folding of the newly synthesized proteins into the correct three-dimensional structure are coupled in cellular compartments of the exocytosis pathway by a process that modulates the phosphorylation level of eukaryotic initiation factor-2alpha (eIF2alpha) in response to a stress signal from the endoplasmic reticulum (ER). Activation of this process leads to reduced rates of initiation of protein translation during ER stress. Here we describe the cloning of perk, a gene encoding a type I transmembrane ER-resident protein. PERK has a lumenal domain that is similar to the ER-stress-sensing lumenal domain of the ER-resident kinase Ire1, and a cytoplasmic portion that contains a protein-kinase domain most similar to that of the known eIF2alpha kinases, PKR and HRI. ER stress increases PERK's protein-kinase activity and PERK phosphorylates eIF2alpha on serine residue 51, inhibiting translation of messenger RNA into protein. These properties implicate PERK in a signalling pathway that attenuates protein translation in response to ER stress.
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0028-0836
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
21
|
|
pubmed:volume |
397
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
271-4
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:9930704-3T3 Cells,
pubmed-meshheading:9930704-Amino Acid Sequence,
pubmed-meshheading:9930704-Animals,
pubmed-meshheading:9930704-COS Cells,
pubmed-meshheading:9930704-Caenorhabditis elegans,
pubmed-meshheading:9930704-Cloning, Molecular,
pubmed-meshheading:9930704-Endoplasmic Reticulum,
pubmed-meshheading:9930704-Escherichia coli,
pubmed-meshheading:9930704-Eukaryotic Initiation Factor-2,
pubmed-meshheading:9930704-Fungal Proteins,
pubmed-meshheading:9930704-Gene Expression Regulation,
pubmed-meshheading:9930704-Humans,
pubmed-meshheading:9930704-Intracellular Membranes,
pubmed-meshheading:9930704-Membrane Glycoproteins,
pubmed-meshheading:9930704-Mice,
pubmed-meshheading:9930704-Molecular Sequence Data,
pubmed-meshheading:9930704-Protein Biosynthesis,
pubmed-meshheading:9930704-Protein Folding,
pubmed-meshheading:9930704-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9930704-Recombinant Fusion Proteins,
pubmed-meshheading:9930704-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9930704-Sequence Homology, Amino Acid,
pubmed-meshheading:9930704-Signal Transduction,
pubmed-meshheading:9930704-eIF-2 Kinase
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase.
|
|
pubmed:affiliation |
Skirball Institute of Biomolecular Medicine, Department of Medicine, NYU School of Medicine, New York 10016, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
