Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

By A. Bertolotti, Yuhong Zhang, L. Hendershot, H. Harding, D. Ron. Nature Cell Biology, 2000

2,890 citations recorded by the source corpus.

Subfields: Cell Biology, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/63c6f13c6854df00464cbea2f4a3ec5ec58cddc2

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. C. Hetz
4. D. Ron
5. J. Malhotra
6. Laurie H. Glimcher
7. Peter Walter
8. M. Schröder

In Immunology

1. R. Kaufman
2. G. Hotamışlıgil
3. D. Ron
4. C. Hetz
5. H. Harding
6. J. Malhotra
7. Junying Yuan
8. Laurie H. Glimcher

In Molecular Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. D. Ron
4. C. Hetz
5. J. Malhotra
6. M. Schröder
7. H. Harding
8. Laurie H. Glimcher

Citations in the corpus

• The unfolded protein response in nutrient sensing and differentiation (2002, background): “In unstressed conditions, Ire1 maintains a mainly monomeric and inactive state by binding to the ER-localized protein chaperone KAR2/BiP/GRP78 (Ref”
• Higher-Order Substrate Recognition of eIF2α by the RNA-Dependent Protein Kinase PKR (2005, neutral): “Indeed, as observed for PKR, dimerization and autophosphorylation appear to be an integral part of PERK, HRI, and GCN2 protein kinase function (Bertolotti et al., 2000; Bauer et al., 2001; Qiu et al., 2001).”
• Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. (2001, methodology): “This might be predicted to increase signaling through parallel, PERK-independentspecific antisera (Bertolotti et al., 2000).”
• The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages (2003, background): “PERK is specifically activated by impaired protein folding in the endoplasmic reticulum lumen, a common outcome of many perturbations of organelle functio”
• Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins (2006, background): “signaling cascades that comprise the UPR [4,64].”
• Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. (2006, background): “UPR signaling is initiated by increased demand for protein-folding capacity, which titrates ER chaperones away from the luminal domains of ER stresssensing proteins, causing their activation (38, 39).”
• The endoplasmic reticulum stress response in immunity and autoimmunity (2008, background): “In the absence of ER stress, the IRE1, PERK and ATF6 proteins are sequestered in inactive complexes with immunoglobulin-heavy-chain-binding protein ( BIP ; also known as GRP78 and HSPA5), an ER-resident chaperon”
• Roles of CHOP/GADD153 in endoplasmic reticulum stress (2004, background): “sensor of unfolded proteins in the ER and regulates the activation of these ER stress transducers.(33,34) All transducers contain a lumenal domain to which BiP can bind.”
• Endoplasmic reticulum stress contributes to beta cell apoptosis in type 2 diabetes (2007, background): “Heat shock 70 kDa protein 5 (HSPA5, previously known as immunoglobulin heavy chain binding protein [BIP]) is central to this process as it serves both as an ER chaperone and a sensor of protein misfolding [10].”