Marciniak, S.J. & Ron, D. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86, 1133–1149 (2006).
Schröder, M. & Kaufman, R.J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739–789 (2005).
Ron, D. & Walter, P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519–529 (2007).
Bernales, S., Papa, F.R. & Walter, P. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 22, 487–508 (2006).
Cox, J.S., Shamu, C.E. & Walter, P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197–1206 (1993).
Mori, K., Ma, W., Gething, M.J. & Sambrook, J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74, 743–756 (1993).
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T. & Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107, 881–891 (2001).
Lee, K. et al. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16, 452–466 (2002).
Calfon, M. et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP–1 mRNA. Nature 415, 92–96 (2002).
Clauss, I.M., Chu, M., Zhao, J.L. & Glimcher, L.H. The basic domain/leucine zipper protein hXBP–1 preferentially binds to and transactivates CRE-like sequences containing an ACGT core. Nucleic Acids Res. 24, 1855–1864 (1996).
Lee, A.H., Iwakoshi, N.N. & Glimcher, L.H. XBP–1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448–7459 (2003).
Sriburi, R., Jackowski, S., Mori, K. & Brewer, J.W. XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J. Cell Biol. 167, 35–41 (2004).
Sriburi, R. et al. Coordinate regulation of phospholipid biosynthesis and secretory pathway gene expression in XBP–1(S)-induced endoplasmic reticulum biogenesis. J. Biol. Chem. 282, 7024–7034 (2007).
Fagone, P. et al. Phospholipid biosynthesis program underlying membrane expansion during B-lymphocyte differentiation. J. Biol. Chem. 282, 7591–7605 (2007).
Ozcan, U. et al. Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis. Mol. Cell 29, 541–551 (2008).
Ozcan, U. et al. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 313, 1137–1140 (2006).
Ozcan, U. et al. Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes. Science 306, 457–461 (2004).
Ozcan, L. et al. Endoplasmic reticulum stress plays a central role in development of leptin resistance. Cell Metab. 9, 35–51 (2009).
Richardson, C.E., Kooistra, T. & Kim, D.H. An essential role for XBP–1 in host protection against immune activation in C. elegans. Nature 463, 1092–1095 (2010).
Martinon, F., Chen, X., Lee, A.H. & Glimcher, L.H. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat. Immunol. 11, 411–418 (2010).
Sado, M. et al. Protective effect against Parkinson′s disease-related insults through the activation of XBP1. Brain Res. 1257, 16–24 (2009).
Kaser, A. et al. XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease. Cell 134, 743–756 (2008).
Koong, A.C., Chauhan, V. & Romero-Ramirez, L. Targeting XBP–1 as a novel anti-cancer strategy. Cancer Biol. Ther. 5, 756–759 (2006).
Nakatani, Y. et al. Involvement of endoplasmic reticulum stress in insulin resistance and diabetes. J. Biol. Chem. 280, 847–851 (2005).
Ozawa, K. et al. The endoplasmic reticulum chaperone improves insulin resistance in type 2 diabetes. Diabetes 54, 657–663 (2005).
Park, S.W. et al. The regulatory subunits of PI3K, p85alpha and p85beta, interact with XBP–1 and increase its nuclear translocation. Nat. Med. 16, 429–437 (2010).
Zhou, Y. et al. Regulation of glucose homeostasis through a XBP–1-FoxO1 interaction. Nat. Med. 17, 356–365 (2011).
Coulthard, L.R., White, D.E., Jones, D.L., McDermott, M.F. & Burchill, S.A. p38(MAPK): stress responses from molecular mechanisms to therapeutics. Trends Mol. Med. 15, 369–379 (2009).
Morrison, D.K. & Davis, R.J. Regulation of MAP kinase signaling modules by scaffold proteins in mammals. Annu. Rev. Cell Dev. Biol. 19, 91–118 (2003).
Chang, L. & Karin, M. Mammalian MAP kinase signalling cascades. Nature 410, 37–40 (2001).
Dong, C., Davis, R.J. & Flavell, R.A. MAP kinases in the immune response. Annu. Rev. Immunol. 20, 55–72 (2002).
Urano, F. et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287, 664–666 (2000).
Matsuzawa, A., Nishitoh, H., Tobiume, K., Takeda, K. & Ichijo, H. Physiological roles of ASK1-mediated signal transduction in oxidative stress- and endoplasmic reticulum stress-induced apoptosis: advanced findings from ASK1 knockout mice. Antioxid. Redox Signal. 4, 415–425 (2002).
Park, S.K., Sanders, B.G. & Kline, K. Tocotrienols induce apoptosis in breast cancer cell lines via an endoplasmic reticulum stress-dependent increase in extrinsic death receptor signaling. Breast Cancer Res. Treat. 124, 361–375 (2010).
Lin, J.H. et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 318, 944–949 (2007).
Tournier, C. et al. MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines. Genes Dev. 15, 1419–1426 (2001).
Kyriakis, J.M. & Avruch, J. Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81, 807–869 (2001).
Schaeffer, H.J. & Weber, M.J. Mitogen-activated protein kinases: specific messages from ubiquitous messengers. Mol. Cell. Biol. 19, 2435–2444 (1999).
Lei, K. et al. The Bax subfamily of Bcl2-related proteins is essential for apoptotic signal transduction by c-Jun NH(2)-terminal kinase. Mol. Cell. Biol. 22, 4929–4942 (2002).
Brancho, D. et al. Mechanism of p38 MAP kinase activation in vivo. Genes Dev. 17, 1969–1978 (2003).
Raingeaud, J., Whitmarsh, A.J., Barrett, T., Derijard, B. & Davis, R.J. MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. Mol. Cell. Biol. 16, 1247–1255 (1996).
Clark, A., Dean, J., Tudor, C. & Saklatvala, J. Post-transcriptional gene regulation by MAP kinases via AU-rich elements. Front. Biosci. 14, 847–871 (2009).
Park, E.J. et al. Dietary and genetic obesity promote liver inflammation and tumorigenesis by enhancing IL-6 and TNF expression. Cell 140, 197–208 (2010).
Olefsky, J.M. & Glass, C.K. Macrophages, inflammation, and insulin resistance. Annu. Rev. Physiol. 72, 219–246 (2010).
Shoelson, S.E., Lee, J. & Goldfine, A.B. Inflammation and insulin resistance. J. Clin. Invest. 116, 1793–1801 (2006).
Solinas, G. & Karin, M. JNK1 and IKKbeta: molecular links between obesity and metabolic dysfunction. FASEB J. 24, 2596–2611 (2010).
Arkan, M.C. et al. IKK-beta links inflammation to obesity-induced insulin resistance. Nat. Med. 11, 191–198 (2005).
Solinas, G. et al. JNK1 in hematopoietically derived cells contributes to diet-induced inflammation and insulin resistance without affecting obesity. Cell Metab. 6, 386–397 (2007).
Hirosumi, J. et al. A central role for JNK in obesity and insulin resistance. Nature 420, 333–336 (2002).
Lee, A.H., Iwakoshi, N.N., Anderson, K.C. & Glimcher, L.H. Proteasome inhibitors disrupt the unfolded protein response in myeloma cells. Proc. Natl. Acad. Sci. USA 100, 9946–9951 (2003).