The cellular response to stress-induced alterations in protein folding in the endoplasmic reticulum

In Vitro and Molecular Toxicology: Journal of Basic and Applied Research

Volumn 11, Issue 1, 1998, Pages 63-71

  Welihinda, Ajith A ^a   Tirasophon, Witoon ^a   Kaufman, Randal J ^a,b  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HISTONE; HISTONE ACETYLTRANSFERASE; MEMBRANE RECEPTOR; MESSENGER RNA; PROTEIN SERINE THREONINE KINASE;

ACETYLATION; CELL NUCLEUS MEMBRANE; CONFERENCE PAPER; DELETION MUTANT; DEPHOSPHORYLATION; ENDOPLASMIC RETICULUM; NONHUMAN; PROTEIN FOLDING; RNA PROCESSING; RNA SPLICING; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION; STRESS; TRANSCRIPTION INITIATION;

ADA; EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0031831369     PISSN: 10979336     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper

References (29)

1. BROWNELL, J.E., ZHOUY, J., RANALLI, T., et al. (1996). Tetrahymena histone acetyletransferase A: A homolog of yeast Gcn5p linking histone acetylation to gene activation. Cell 84, 843-851.
2. CANDAU, R., ZHOU, J.X., ALLIS, C.D., BERGER, S.L. (1997). Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. Embo J 16, 555-565.
3. CHANG, S.C., ERWIN, A.E., and LEE, A.S. (1989). Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors. Mol. Cell Biol. 9, 2153-2162.
4. CLARK, M.W., and ABELSON, J. (1987). The sub-nuclear localization of tRNA ligase in yeast. J. Cell Biol. 105, 1515-1526.
5. COX, J.S., and WALTER, P. (1996). A novel mechanism for regulating activity of a transcription factor that controlsthe unfolded protein response. Cell 87, 391-404.
6. COX, J.S., SHAMU, C.E., and WALTER, P. (1993). Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197-1206.
7. FLYNN, G.C., POHL, J., FLOCCO, M.D., and ROTHMAN, J.E. (1991). Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730.
8. GEORGAKOPOULOS, T., and THIREOS, G. (1992). Two distinct yeast transcriptional activators require the function of the Gcn5 protein to promote normal levels of transcription. EMBO J. 11, 4145-4152.
9. HARTL, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
10. HORIUCHI, J., SILVERMAN, N., PINA, B., MARCUS, G.A., and GUARENTE, L. (1997). ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3. Mol. Cell Biol. 17, 3220-3228.
11. KASSENBROCK, C.K., and KELLY, R.B. (1989). Interaction of heavy chain binding (BiP/GRP78) with adenine nucleotides. EMBO J. 8, 1461-1467.
12. KAWAHARA, T., YANAGI, H., YURA, T., and MORI, K. (1997). Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein response. Mol. Biol. Cell 8, 1845-1862.
13. LA MANTIA, M., MIURA, T., TACHIKAWA, H., KAPLAN, H.A., LENNARZ, W.J., and MIZUNAGA, T. (1991). Glycosylation site binding proteins and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc. Natl. Acad. Sci. U.S.A. 88, 4453-4457.
14. MARCUS, G.A., SILVERMAN, N., BERGER, S.L., HORIUCHI, J., and GUARENTE, L. (1994). Functional similarity and physical association between GCN5 and ADA2: Putative transcriptional adaptors. EMBO J. 13, 4807-4815.
15. MARCUS, G.A., HORIUCHI, J., SILVERMAN, N., and GUARENTE, L. (1996). ADA5/SPT20 links the ADA and SPT genes, which are involved in yeast transcription. Mol. Cell. Biol. 16, 3197-3205.
16. MORI, K., SANT, A., KOHNO, K., NORMINGTON, K., GETHING, M.J., and SAMBROOK, J.F. (1992). A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11, 2583-2593.
17. MORI, K., MA, W., GETHING, M.J., and SAMBROOK, J. (1993). A transmembrane protein with a cdc2+/ CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74, 743-756.
18. MORI, K., KAWAHARA, T., YOSHIDA, H,. YANAGI, H., and YURA, T. (1996). Signalling from endoplasmic reticulum to nucleus: Transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway. Genes Cells. 1, 803-817.
19. MORRIS, J.A., DORNER, A.J., EDWARDS, C.A., HENDERSHOT, L.M., and KAUFMAN, R.J. (1997). Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J. Biol. Chem. 272, 4327-4334.
20. MUNRO, S., and PELHAM, H.R. (1986). An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 46, 291-300.
21. PALLEROS, D.R., REID, K.D,. SHI, L., WELCH, W.J., and FINK, A.L. (1993). ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature 346, 664-666.
22. SHAMU, C.E. (1997). Signal transduction: Splicing together the unfolded-protein response. Current Biol. 7, R67-R70.
23. SHAMU, C.E., and WALTER, P. (1996). Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028-3039.
24. SIDRAUSKI, C., and WALTER, P. (1997). The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90, 1031-1039.
25. SIDRAUSKI, C., COX, J.S., and WALTER, P. (1996). tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87, 405-413.
26. WEI, J., and HENDERSHOT, L.M. (1995). Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. J. Biol. Chem. 270, 26670-26676.
27. WELIHINDA, A.A., and KAUFMAN, R.J. (1996). The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and transphosphorylation of Ire1p (Ern1p) are required for kinase activation. J. Biol. Chem. 271, 18181-18187.
28. WELIHINDA, A.A., TIRASOPHON, W., GREEN, S.R., and KAUFMAN, R.J. (1997). Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p. Proc. Natl. Acad. Sci. U.S.A. 94, 4289-4294.
29. WELIHINDA, A.A., TIRASOPHON, W., GREEN, S.R., and KAUFMAN, R.J. (1998). Protein serine/threonine phosphatase P+ C2p negatively regulates the unfolded-protein response by dephosphorylating Ire1p. Mol. Cell Biol. 18.