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Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
Howard Hughes Medical Institute · Harvard University · +2 more institutions
Abstract
Accumulation of misfolded protein in the endoplasmic reticulum (ER) triggers an adaptive stress response-termed the unfolded protein response (UPR)-mediated by the ER transmembrane protein kinase and endoribonuclease inositol-requiring enzyme-1alpha (IRE1alpha). We investigated UPR signaling events in mice in the absence of the proapoptotic BCL-2 family members BAX and BAK [double knockout (DKO)]. DKO mice responded abnormally to tunicamycin-induced ER stress in the liver, with extensive tissue damage and decreased expression of the IRE1 substrate X-box-binding protein 1 and its target genes. ER-stressed DKO cells showed deficient IRE1alpha signaling. BAX and BAK formed a protein complex with the cytosolic…
Citation impact
- FWCI
- 16.75
- Percentile
- 100%
- References
- 32
Authors
11- CHClaudio HetzCorresponding
Howard Hughes Medical Institute, Harvard University, Dana-Farber Cancer Institute, Brandeis University
- PBPaula Bernasconi
Howard Hughes Medical Institute, Harvard University, Dana-Farber Cancer Institute, Brandeis University
- JKJill K. Fisher
Howard Hughes Medical Institute, Harvard University, Dana-Farber Cancer Institute, Brandeis University
- ALAnn–Hwee Lee
Howard Hughes Medical Institute, Harvard University, Dana-Farber Cancer Institute, Brandeis University
- MCMichael C. Bassik
Howard Hughes Medical Institute, Harvard University, Dana-Farber Cancer Institute, Brandeis University
Topics & keywords
- Unfolded protein response
- Fight-or-flight response
- Cell biology
- Endoplasmic reticulum
- Chemistry
- Biology
- Genetics
- Gene