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

Lee, A. Mammalian stress response: induction of the glucose-regulated protein family. Curr. Biol. 4, 267–273 ( 1992).

Brostrom, C. O. & Brostrom, M. A. Regulation of translational initiation during cellular responses to stress. Prog. Nucleic Acid Res. Mol. Biol. 58, 79– 125 (1998).

Chapman, R., Sidrauski, C. & Walter, P. Intracellular signaling from the endoplasmic reticulum to the nucleus. Annu. Rev. Cell Dev. Biol. 14, 459–485 (1998).

Kaufman, R. J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211–1233 ( 1999).

Tirasophon, W., Welihinda, A. A. & Kaufman, R. J. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12, 1812–1824 (1998).

Wang, X. Z. et al. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17, 5708– 5717 (1998).

Shi, Y. et al. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol. Cell Biol. 18, 7499–7509 (1998).

Harding, H., Zhang, Y. & Ron, D. Translation and protein folding are coupled by an endoplasmic reticulum resident kinase. Nature 397, 271– 274 (1999).

Munro, S. & Pelham, H. R. An Hsp70-like protein in the ER: identity with the 78 kDa glucose- regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291– 300 (1986).

Wei, J. & Hendershot, L. M. Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. J. Biol. Chem. 270, 26670 –26676 (1995).

Hebert, D. N., Simons, J. F., Peterson, J. R. & Helenius, A. Calnexin, calreticulin, and Bip/Kar2p in protein folding. Cold Spring Harb. Symp. Quant. Biol. 60, 405– 415 (1995).

Dorner, A., Wasley, L. & Kaufman, R. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11, 1563– 1571 (1992).

Wang, et al. Signals from the stressed endoplasmic reticulum induce C/EBP homologous protein (CHOP/GADD153). Mol. Cell Biol. 16, 4273 –4280 (1996).

Shamu, C. E. & Walter, P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028– 3039 (1996).

Welihinda, A. A. & Kaufman, R. J. The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation. J. Biol. Chem. 271, 18181– 18187 (1996).

Langland, J. O. & Jacobs, B. L. Cytosolic double-stranded RNA-dependent protein kinase is likely a dimer of partially phosphorylated Mr 66,000 subunits. J. Biol. Chem. 267 , 10729–10736 (1992).

Reinhard, C., Shamoon, B., Shyamala, V. & Williams, L. T. Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2. EMBO J. 16, 1080– 1092 (1997).

Bukau, B. & Horwich, A. L. The Hsp70 and Hsp60 chaperone machines. Cell 92, 351– 366 (1998).

Matlack, K. E., Misselwitz, B., Plath, K. & Rapoport, T. A. BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97, 553–564 (1999).

Liberek, K., Galitski, T. P., Zylicz, M. & Georgopoulos, C. The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor. Proc. Natl Acad. Sci. USA 89, 3516–3520 (1992).

Gamer, J., Bujard, H. & Bukau, B. Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32 . Cell 69, 833–842 (1992).

Tomoyasu, T., Ogura, T., Tatsuta, T. & Bukau, B. Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli. Mol. Microbiol. 30, 567–581 (1998).

Morimoto, R. I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators . Genes Dev. 12, 3788–3796 (1998).

Zou, J., Guo, Y., Guettouche, T., Smith, D. F. & Voellmy, R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94, 471–480 ( 1998).

Straus, D. B., Walter, W. A. & Gross, C. A. The activity of sigma 32 is reduced under conditions of excess heat shock protein production in Escherichia coli. Genes Dev. 3, 2003–2010 (1989).

Kohno, K., Normington, K., Sambrook, J., Gething, M. J. & Mori, K. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell Biol. 13, 877–890 (1993).

Freiden, P. J., Gaut, J. R. & Hendershot, L. M. Interconversion of three differentially modified and assembled forms of BiP. EMBO J. 11, 63–70 (1992).

Hendershot, L. M. et al. In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum. Mol. Biol. Cell 6, 283–296 ( 1995).

Bertolotti, A. et al. EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes. Mol. Cell Biol. 18, 1489–1497 (1998).