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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Hetz, C. et al.

Hetz, Bernasconi, Fisher, Lee, Bassik, Antonsson, Brandt, Iwakoshi, Schinzel, Glimcher, Korsmeyer,

Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha.

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 domain of IRE1alpha that was essential for IRE1alpha activation. Thus, BAX and BAK function at the ER membrane to activate IRE1alpha signaling and to provide a physical link between members of the core apoptotic pathway and the UPR.[1]

References

Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha. Hetz, C., Bernasconi, P., Fisher, J., Lee, A.H., Bassik, M.C., Antonsson, B., Brandt, G.S., Iwakoshi, N.N., Schinzel, A., Glimcher, L.H., Korsmeyer, S.J. Science (2006) [Pubmed]

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