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Signal integration in the endoplasmic reticulum unfolded protein response
Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and lipids. Expand
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled proteins advance from… Expand
Regulated translation initiation controls stress-induced gene expression in mammalian cells.
Protein kinases that phosphorylate the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) are activated in stressed cells and negatively regulate protein synthesis, resulting in the induction of the downstream gene CHOP (GADD153). Expand
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
- A. Bertolotti, Yuhong Zhang, L. Hendershot, H. Harding, D. Ron
- Chemistry, Medicine
- Nature Cell Biology
- 1 June 2000
It is shown that the lumenal domains of these two proteins are functionally interchangeable in mediating an ER stress response and that, in unstressed cells, both lumenAL domains form a stable complex with the ER chaperone BiP. Expand
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
The cloning of perk is described, a gene encoding a type I transmembrane ER-resident protein that contains a protein-kinase domain most similar to that of the known eIF2α kinases, PKR and HRI that implicate PERK in a signalling pathway that attenuates protein translation in response to ER stress. Expand
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
It is demonstrated that mutations in either ire-1 or the transcription-factor-encoding xbp-1 gene abolished the UPR in Caenorhabditis elegans, suggesting that physiological ER load regulates a developmental decision in higher eukaryotes. Expand
An integrated stress response regulates amino acid metabolism and resistance to oxidative stress.
A signaling pathway initiated by eIF2alpha phosphorylation protects cells against metabolic consequences of ER oxidation by promoting the linked processes of amino acid sufficiency and resistance to oxidative stress. Expand
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes… Expand
Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2.
- J. Nangalia, C. Massie, +49 authors A. Green
- Biology, Medicine
- The New England journal of medicine
- 18 December 2013
Somatic mutations in the endoplasmic reticulum chaperone CALR were found in a majority of patients with myeloproliferative neoplasms with nonmutated JAK2, a finding consistent with its role as an initiating mutation in some patients. Expand
CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum.
This work finds that CHOP directly activates GADD34, which promotes ER client protein biosynthesis by dephosphorylating phospho-Ser 51 of the alpha-subunit of translation initiation factor 2 (eIF2alpha) in stressed cells, and protects cells from ER stress by decreasing client protein load and changing redox conditions within the organelle. Expand