Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
Article Abstract:
The cloning of the perk gene encoding a type I transmembrane ER-resident protein is described. PERK's lumenal domain is similar to the stress sensing domain of the Ire1 kinase. ER stress raises the protein-kinase activity of PERK, and PERK phosphorylates eIF2alpha on serine residue 51, preventing messenger RNA translation into protein. This implicates PERK in a signalling pathway, in response to ER stress.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
Article Abstract:
Cotransin, a small molecule that inhibits protein translocation into the endoplasmic reticulum is described. Cotransin acts in a signal-sequence-discriminatory manner to prevent the stable insertion of select nascent chains into the Sec61 translocation channel.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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- Abstracts: Quality control in the endoplasmic reticulum protein factory. Protein folding and misfolding
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