A novel ER stress transducer, OASIS, expressed in astrocytes

Antioxidants and Redox Signaling

Volumn 9, Issue 5, 2007, Pages 563-571

  Saito, Atsushi ^a,b   Hino, Shin Ichiro ^a   Murakami, Tomohiko ^a,b   Kondo, Shinichi ^a   Imaizumi, Kazunori ^a  

^a UNIVERSITY OF MIYAZAKI   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OASIS; UNCLASSIFIED DRUG;

ASTROCYTE; CELL POPULATION; CELL PROLIFERATION; CELL TYPE; ENDOPLASMIC RETICULUM; GLIA CELL; NERVE CELL NECROSIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; REVIEW; SIGNAL TRANSDUCTION;

ACTIVATING TRANSCRIPTION FACTOR 6; ANIMALS; ASTROCYTES; CELL MEMBRANE; CYCLIC AMP RESPONSE ELEMENT-BINDING PROTEIN; ENDOPLASMIC RETICULUM; GENE EXPRESSION REGULATION; NERVE TISSUE PROTEINS; PROTEIN FOLDING; SIGNAL TRANSDUCTION; TRANS-ACTIVATION (GENETICS);

EID: 34247152063     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.1520     Document Type: Review

References (53)

1. Adham IM, Eck TJ, Mierau K, Muller N, Sallam MA, Paprotta I, Schubert S, Hoyer-Fender S, and Engel W. Reduction of spermatogenesis but not fertility in Creb314-deficient mice. Mol Cell Biol 25: 7657-7664, 2005.
2. Bertolotti A, Zhang Y, Hendershot LM, Harding HP, and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2: 326-332, 2000.
3. Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM, and Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511, 2002.
4. Calfon M, Zeng H, Urano F, Till JH, Hubbard SR, Harding HP, Clark SG, and Ron D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415: 92-96, 2002.
5. DenBoer LM, Hardy-Smith PW, Hogan MR, Cockram GP, Audas TE, and Lu R. Luman is capable of binding and activating transcription from the unfolded protein response element. Biochem Biophys Res Commun 331: 113-119, 2005.
6. Espenshade PJ, Cheng D, Goldstein JL, Brown MS. Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins. J Biol Chem 274: 22795-22804, 1999.
7. Gelman MS and Kopito RR. Rescuing protein conformation: prospects for pharmacological therapy in cystic fibrosis. J Clin Invest 110: 1591-1597, 2002.
8. Hai T and Hartman MG. The molecular biology and nomenclature of the activating transcription factor/cAMP responsive element binding family of transcription factors: activating transcription factor proteins and homeostasis. Gene 273: 1-11, 2001.
9. Harding HP, Zhang Y, and Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397: 271-274, 1999.
10. Harding HP, Zhang Y, Bertolotti A, Zeng H, and Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 5: 897-904, 2000.
11. Haze K, Yoshida H, Yanagi H, Yura T, and Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10: 3787-3799, 1999.
12. Honma Y, Kanazawa K, Mori T, Tanno Y, Tojo M, Kiyosawa H, Takeda J, Nikaido T, Tsukamoto T, Yokoya S, and Wanaka A. Identification of a novel gene, OASIS, which encodes for a putative CREB/ATF family transcription factor in the long-term cultured astrocytes and gliotic tissue. Brain Res Mol Brain Res 69: 93-103, 1999.
13. Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, and Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105: 891-902, 2001.
14. Imaizumi K, Katayama T, and Tohyama M. Presenilin and the UPR. Nat Cell Biol 3: E104, 2001.
15. Katayama T, Imaizumi K, Sato N, Miyoshi K, Kudo T, Hitomi J, Morihara T, Yoneda T, Gomi F, Mori Y, Nakano Y, Takeda J, Tsuda T, Itoyama Y, Murayama O, Takashima A, St George-Hyslop P, Takeda M, and Tohyama M. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nat Cell Biol 1: 479-485, 1999.
16. Kaufman RJ. A trip to the ER: coping with stress. Trends Cell Biol 14: 20-28, 2004.
17. Kondo S, Murakami T, Tatsumi K, Ogata M, Kanemoto S, Otori K, Iseki K, Wanaka A, and Imaizumi K. OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes. Nat Cell Biol 7: 186-194, 2005.
18. Kouroku Y, Fujita E, Jimbo A, Kikuchi T, Yamagata T, Momoi MY, Kominami E, Kuida K, Sakamaki K, Yonehara S, and Momoi T. Polyglutamine aggregates stimulate ER stress signals and caspase-12 activation. Hum Mol Gene 11: 1505-1515, 2002.
19. Li LJ, Li X, Ferrario A, Rucker N, Liu ES, Wong S, Gomer CJ, and Lee AS. Establishment of a Chinese hamster ovary cell line that expresses grp78 antisense transcripts and suppresses A23187 induction of both GRP78 and GRP94. J Cell Physiol 153: 575-582, 1992.
20. Liu CY, Schroder M, and Kaufman RJ. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J Biol Chem 275: 24881-24885, 2000.
21. Lomas DA and Mahadeva R. Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 110: 1585-1590, 2002.
22. Mori K. Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101: 451-454, 2000.
23. Murakami T, Kondo S, Ogata M, Kanemoto S, Saito A, Wanaka A, and Imaizumi K. Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress. J Neurochem 96: 1090-1100, 2006.
24. Nagamori I, Yabuta N, Fujii T, Tanaka H, Yomogida K, Nishimune Y, and Nojima H. Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway. Genes Cells 10: 575-594, 2005.
25. Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, and Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403: 98-103, 2000.
26. Newman JR and Keating AE. Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 300: 2097-2101, 2003.
27. Nikaido T, Yokoya S, Mori T, Hagino S, Iseki K, Zhang Y, Takeuchi M, Takaki H, Kikuchi S, and Wanaka A. Expression of the novel transcription factor OASIS, which belongs to the CREB/ATF family, in mouse embryo with special reference to bone development. Histochem Cell Biol 116: 141-148, 2001.
28. Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, Hori S, Kakizuka A, and Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev 16:1345-1355, 2002.
29. Omori Y, Imai J, Watanabe M, Komatsu T, Suzuki Y, Kataoka K, Watanabe S, Tanigami A, and Sugano S. CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF family and functioning via the box-B element with a liver-specific expression. Nucleic Acids Res 29: 2154-2162, 2001.
30. Omori Y, Imai J, Suzuki Y, Watanabe S, Tanigami A, and Sugano S. OASIS is a transcriptional activator of CREB/ATF family with a transmembrane domain. Biochem Biophys Res Commun 293: 470-477, 2002.
31. Pechan PA, Chowdhury K, and Seifert W. Free radicals induce gene expression of NGF and bFGF in rat astrocyte culture. Neuroreport 3: 469-472.
32. Perlmutter DH. Liver injury in alpha1-antitrypsin deficiency: an aggregated protein induces mitochondrial injury. J Clin Invest 110: 1579-1583, 2002.
33. Podust LM, Krezel AM, and Kim Y. Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA. J Biol Chem 276: 505-513, 2001.
34. Raggo C, Rapin N, Stirling J, Gobeil P, Smith-Windsor E, O'Hare P, and Misra V. Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol 22: 5639-5649, 2002.
35. Ridet JL, Malhotra SK, Privat A, and Gage FH. Reactive astrocytes: cellular and molecular cues to biological function. Trends Neurosci 20: 570-577, 1997.
36. Ron D. Translational control in the endoplasmic reticulum stress response. J Clin Invest 110: 1383-1388, 2002.
37. Roy B and Lee AS. The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complex. Nucleic Acids Res 27: 1437-1443, 1999.
38. Sakai J, Rawson RB, Espenshade PJ, Cheng D, Seegmiller AC, Goldstein JL, and Brown MS. Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol Cell 2: 505-514, 1998.
39. Scheuner D, Song B, McEwen E, Liu C, Laybutt R, Gillespie P, Saunders T, Bonner-Weir S, and Kaufman RJ. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell 7: 1165-1176, 2001.
40. Schroder M and Kaufman RJ. The mammalian unfolded protein response. Annu Rev Biochem 74: 739-789, 2005.
41. Shen X, Ellis RE, Lee K, Liu CY, Yang K, Solomon A, Yoshida H, Morimoto R, Kurnit DM, Mori K, and Kaufman RJ. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 107: 893-903, 2001.
42. Shen J, Chen X, Hendershot L, and Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 3: 99-111, 2002.
43. Sugawara S, Takeda K, Lee A, and Dennert G. Suppression of stress protein GRP78 induction in tumor B/C10ME eliminates resistance to cell mediated cytotoxicity. Cancer Res 53: 6001-6005, 1993.
44. Terro F, Czech C, Esclaire F, Elyaman W, Yardin C, Baclet MC, Touchet N, Tremp G, Pradier L, and Hugon J. Neurons overexpressing mutant presenilin-1 are more sensitive to apoptosis induced by endoplasmic reticulum-Golgi stress. J Neurosci Res 69: 530-539, 2002.
45. Tirasophon W, Welihinda AA, and Kaufman RJ. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. 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.
46. Trojanowski JQ. Tauists, Baptists, Syners, Apostates, and new data. Ann Neurol 52: 263-265, 2002.
47. Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, and Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J 17: 5708-5717, 1998.
48. Ye J, Rawson RB, Komuro R, Chen X, Dave UP, Prywes R, Brown MS, and Goldstein JL. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6: 1355-1364, 2000.
49. Yoshida H, Haze K, Yanagi H, Yura T, and Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J Biol Chem 273: 33741-33749, 1998.
50. Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M, and Mori K. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 20: 6755-6767, 2000.
51. Yoshida H, Matsui T, Yamamoto A, Okada T, and 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.
52. Yoshida H, Matsui T, Hosokawa N, Kaufman RJ, Nagata K, and Mori K. A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 4: 265-271, 2003.
53. Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski DT, Back SH, and Kaufman RJ. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 124: 587-599, 2006.