Novel Cis-acting element GASE regulates transcriptional induction by the Golgi stress response

Cell Structure and Function

Volumn 36, Issue 1, 2011, Pages 1-12

  Oku, Masaya ^a   Tanakura, Soichiro ^b   Uemura, Aya ^a   Sohda, Miwa ^c   Misumi, Yoshio ^d   Taniguchi, Mai ^b   Wakabayashi, Sadao ^b   Yoshida, Hiderou ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF HYOGO   (Japan)

^c NIIGATA UNIVERSITY GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES   (Japan)

^d FUKUOKA UNIVERSITY   (Japan)

Author keywords

ER stress response; Golgi apparatus; Golgi stress response; Unfolded protein response

Indexed keywords

GIANTIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONSENSUS SEQUENCE; CONTROLLED STUDY; DNA RESPONSIVE ELEMENT; GCP60 GENE; GENE; GENE EXPRESSION; GOLGI APPARATUS STRESS RESPONSE ELEMENT; GOLGI COMPLEX; GOLGI STRESS RESPONSE; HELA CELL; LYSOSOME; PRIORITY JOURNAL; SIAT4A GENE; STRESS; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION;

EUKARYOTA; MAMMALIA;

EID: 79953887786     PISSN: 03867196     EISSN: 13473700     Source Type: Journal    
DOI: 10.1247/csf.10014     Document Type: Article

References (45)

1. Band, A.M. and Kuismanen, E. 2005. Localization of plasma membrane t-SNAREs syntaxin 2 and 3 in intracellular compartments. BMC Cell Biol., 6: 26.
2. Berger, E.G. and Roth, J. 1997. The Golgi Apparatus. Birkheuser Verlag, Basel.
3. Bommiasamy, H., Back, S.H., Fagone, P., Lee, K., Meshinchi, S., Vink, E., Sriburi, R., Frank, M., Jackowski, S., Kaufman, R.J., and Brewer, J.W. 2009. ATF6alpha induces XBP1-independent expansion of the endoplasmic reticulum. J. Cell Sci., 122: 1626-1636.
4. Bransburg-Zabary, S., Nachliel, E., and Gutman, M. 1996. Utilization of monensin for detection of microdomains in cholesterol containing membrane. Biochim Biophys Acta, 1285: 146-154.
5. Chakravarthy, M.V., Lodhi, I.J., Yin, L., Malapaka, R.R., Xu, H.E., Turk, J., and Semenkovich, C.F. 2009. Identification of a physiologically relevant endogenous ligand for PPARalpha in liver. Cell, 138: 476-488.
6. Clermont, Y., Xia, L., Rambourg, A., Turner, J.D., and Hermo, L. 1993. Structure of the Golgi apparatus in stimulated and nonstimulated acinar cells of mammary glands of the rat. Anat. Rec., 237: 308-317.
7. Dinter, A. and Berger, E.G. 1998. Golgi-disturbing agents. Histochem. Cell Biol., 109: 571-590.
8. Fujita, Y., Ohama, E., Takatama, M., Al-Sarraj, S., and Okamoto, K. 2006. Fragmentation of Golgi apparatus of nigral neurons with alpha-synuclein-positive inclusions in patients with Parkinson's disease. Acta Neuropathol., 112: 261-265.
9. Grinde, B. 1983. Effect of carboxylic ionophores on lysosomal protein degradation in rat hepatocytes. Exp. Cell Res., 149: 27-35.
10. Haynes, C.M., Petrova, K., Benedetti, C., Yang, Y., and Ron, D. 2007. ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell, 13: 467-480.
11. Haynes, C.M., Yang, Y., Blais, S.P., Neubert, T.A., and Ron, D. 2010. The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol. Cell, 37: 529-540.
12. Hu, Z., Zeng, L., Huang, Z., Zhang, J., and Li, T. 2007. The study of Golgi apparatus in Alzheimer's disease. Neurochem. Res., 32: 1265-1277.
13. Huynh, D.P., Yang, H.T., Vakharia, H., Nguyen, D., and Pulst, S.M. 2003. Expansion of the polyQ repeat in ataxin-2 alters its Golgi localization, disrupts the Golgi complex and causes cell death. Hum. Mol. Genet., 12: 1485-1496.
14. Jeffries, T.R., Dove, S.K., Michell, R.H., and Parker, P.J. 2004. PtdInsspecific MPR pathway association of a novel WD40 repeat protein, WIPI49. Mol. Biol. Cell, 15: 2652-2663.
15. Jellinger, K.A. 2009. Recent advances in our understanding of neurodegeneration. J. Neural Transm., 116: 1111-1162.
16. Karpichev, I.V., Luo, Y., Marians, R.C., and Small, G.M. 1997. A complex containing two transcription factors regulates peroxisome pro-liferation and the coordinate induction of beta-oxidation enzymes in Saccharomyces cerevisiae. Mol. Cell. Biol., 17: 69-80.
17. Kitagawa, H. and Paulson, J.C. 1994. Cloning of a novel alpha 2,3- sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J. Biol. Chem., 269: 1394-1401.
18. Kohno, K. 2010. Stress-sensing mechanisms in the unfolded protein response: similarities and differences between yeast and mammals. J. Biochem., 147: 27-33.
19. Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., and Mizushima, N. 2004. The role of autophagy during the early neonatal starvation period. Nature, 432: 1032-1036.
20. Lee, A.H., Chu, G.C., Iwakoshi, N.N., and Glimcher, L.H. 2005. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J., 24: 4368-4380.
21. Mori, K. 2009. Signalling pathways in the unfolded protein response: development from yeast to mammals. J. Biochem., 146: 743-750.
22. Phelps, C., Gburcik, V., Suslova, E., Dudek, P., Forafonov, F., Bot, N., MacLean, M., Fagan, R.J., and Picard, D. 2006. Fungi and animals may share a common ancestor to nuclear receptors. Proc. Natl. Acad. Sci. USA, 103: 7077-7081.
23. Price, B.D., Mannheim-Rodman, L.A., and Calderwood, S.K. 1992. Brefeldin A, thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J. Cell. Physiol., 152: 545-552.
24. Rambourg, A., Clermont, Y., Chretien, M., and Olivier, L. 1993. Modula- tion of the Golgi apparatus in stimulated and nonstimulated prolactin cells of female rats. Anat. Rec., 235: 353-362.
25. Reddy, J.K. and Hashimoto, T. 2001. Peroxisomal beta-oxidation and peroxisome proliferator-activated receptor alpha: an adaptive metabolic system. Annu. Rev. Nutr., 21: 193-230.
26. Reimold, A.M., Iwakoshi, N.N., Manis, J., Vallabhajosyula, P., Szomolanyi- Tsuda, E., Gravallese, E.M., Friend, D., Grusby, M.J., Alt, F., and Glimcher, L.H. 2001. Plasma cell differentiation requires the transcription factor XBP-1. Nature, 412: 300-307.
27. Ron, D. and Walter, P. 2007. Signal integration in the endoplasmicreticulum unfolded protein response. Nat. Rev. Mol. Cell Biol., 8: 519-529.
28. Ryan, M.T. and Hoogenraad, N.J. 2007. Mitochondrial-nuclear communications. Annu. Rev. Biochem., 76: 701-722.
29. Sakaguchi, T., Leser, G.P., and Lamb, R.A. 1996. The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus. J. Cell Biol., 133: 733-747.
30. Sardiello, M., Palmieri, M., di Ronza, A., Medina, D.L., Valenza, M., Gennarino, V.A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R.S., Banfi, S., Parenti, G., Cattaneo, E., and Ballabio, A. 2009. A gene network regulating lysosomal biogenesis and function. Science, 325: 473-477.
31. Sbodio, J.I., Hicks, S.W., Simon, D., and Machamer, C.E. 2006. GCP60 preferentially interacts with a caspase-generated golgin-160 fragment. J. Biol. Chem., 281: 27924-27931.
32. Sbodio, J.I. and Machamer, C.E. 2007. Identification of a redox-sensitive cysteine in GCP60 that regulates its interaction with golgin-160. J. Biol. Chem., 282: 29874-29881.
33. Scheuner, D. and Kaufman, R.J. 2008. The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes. Endocr. Rev., 29: 317-333.
34. Sohda, M., Misumi, Y., Yamamoto, A., Yano, A., Nakamura, N., and Ikehara, Y. 2001. Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J. Biol. Chem., 276: 45298-45306.
35. Sriburi, R., Jackowski, S., Mori, K., and Brewer, J.W. 2004. XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J. Cell Biol., 167: 35-41.
36. Tartakoff, A.M. 1983. Perturbation of the structure and function of the Golgi complex by monovalent carboxylic ionophores. Methods Enzymol., 98: 47-59.
37. Yoshida, H. 2007a. ER stress and diseases. FEBS J., 274: 630-658.
38. Yoshida, H. 2007b. Unconventional splicing of XBP-1 mRNA in the unfolded protein response. Antioxid. Redox Signal., 9: 2323-2333.
39. Yoshida, H. 2009. ER stress response, peroxisome proliferation, mito- chondrial unfolded protein response and Golgi stress response. IUBMB Life, 61: 871-879.
40. Yoshida, H., Haze, K., Yanagi, H., Yura, T., and Mori, K. 1998. 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.
41. Yoshida, H., Matsui, T., Hosokawa, N., Kaufman, R.J., Nagata, K., and Mori, K. 2003. A time-dependent phase shift in the mammalian unfolded protein response. Dev. Cell, 4: 265-271.
42. Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., and Mori, K. 2001a. 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.
43. Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M., and Mori, K. 2001b. Endoplasmic reticulum stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6alpha and 6beta that activates the mammalian unfolded protein response. Mol. Cell. Biol., 21: 1239-1248.
44. Yoshida, H., Uemura, A., and Mori, K. 2009. pXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation. Cell Struct. Funct., 34: 1-10.
45. Zeevaert, R., Foulquier, F., Jaeken, J., and Matthijs, G. 2008. Deficiencies in subunits of the Conserved Oligomeric Golgi (COG) complex define a novel group of Congenital Disorders of Glycosylation. Mol. Genet. Metab., 93: 15-21.