FAD-linked presenilin-1 mutants impede translation regulation under ER stress

Biochemical and Biophysical Research Communications

Volumn 296, Issue 2, 2002, Pages 313-318

  Yasuda, Yuka ^a   Kudo, Takashi ^a   Katayama, Taiichi ^a   Imaizumi, Kazunori ^b   Yatera, Misako ^a   Okochi, Masayasu ^a   Yamamori, Hidenaga ^a   Matsumoto, Naohiko ^a   Kida, Takayuki ^a   Fukumori, Akio ^a   Okumura, Masayo ^b   Tohyama, Masaya ^a   Takeda, Masatoshi ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

eIF2 ; ER stress; Familial Alzheimer's disease (FAD); PERK; Presenilin 1 (PS1); Unfolded protein response (UPR)

Indexed keywords

CHAPERONE; ENDOPLASMIC RETICULUM RESIDENT TRANSMEMBRANE PROTEIN KINASE; EUKARYOTIC INITIATION FACTOR 2 ALPHA; FLAVINE ADENINE NUCLEOTIDE; INITIATION FACTOR; MUTANT PROTEIN; PHOSPHOTRANSFERASE; PRESENILIN 1; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL ACTIVITY; CELL MUTANT; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; ENZYME ACTIVITY; GENE MUTATION; MOLECULE; MOUSE; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN SYNTHESIS; STRESS; TRANSLATION REGULATION;

ALZHEIMER DISEASE; ANIMALS; CELLS, CULTURED; EIF-2 KINASE; ENDOPLASMIC RETICULUM; EUKARYOTIC INITIATION FACTOR-2; FIBROBLASTS; HUMANS; MEMBRANE PROTEINS; MICE; MICE, TRANSGENIC; MUTATION; PRESENILIN-1; PROTEIN BIOSYNTHESIS; SIGNAL TRANSDUCTION;

EUKARYOTA;

EID: 0036386967     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00859-8     Document Type: Article

References (27)

1. E.I. Rogaev, R. Sherrington, E.A. Rogaeva, G. Levesque, et al., Familial Alzheimer's disease in kinders with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene, Nature 376 (1995) 775-778.
2. R. Sherrington, E.I. Rogaev, Y. Liang, E.A. Rogaeva, G. Levesque, et al., Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease, Nature 375 (1995) 754-760.
3. P.H.St. George-Hyslop, J. Haines, E. Rogaev, M. Mortilla, G. Vaula, et al., Genetic evidence for a novel familial Alzheimer's disease locus on chromosome 14, Nat. Genet. 2 (1992) 330-334.
4. E. Levy-Lahad, E.M. Wijsman, E. Nemens, L. Anderson, et al., A familial Alzheimer's disease locus on chromosome 1, Science 269 (1995) 970-973.
5. E. Levy-Lahad, W. Wasco, P.D.M. Poorkaj, et al., Candidate gene for the chromosome 1 familial Alzheimer's disease locus, Science 269 (1995) 973-977.
6. D.R. Borchelt, G. Thinakaran, C.B. Eckman, et al., Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo, Neuron 17 (1996) 1005-1013.
7. C. Duff, K. Eckman, C. Zehr, et al., Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1, Nature 24 (1996) 710-713.
8. J. Walter, A. Capell, J. Grunberg, et al., The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum, Mol. Med. 2 (1996) 673-691.
9. J.G. Culvenor, F. Maher, G. Evin, et al., Alzheimer's disease-associated presenilin 1 in neuronal cells: evidence for localization to the endoplasmic reticulum-Golgi intermediate compartment, J. Neurosci. Res. 49 (1997) 719-731.
10. W.G. Annaert, L. Levesque, K. Craessaerts, et al., Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-golgi compartments of hippocampal neurons, J. Cell Biol. 147 (1999) 277-294.
11. R.J. Kaufman, Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls, Genes Dev. 13 (1999) 1211-1233.
12. K. Mori, Tripartite management of unfolded proteins in the endoplasmic reticulum, Cell 101 (2000) 451-454.
13. C.O. Brostrom, M.A. Brostrom, Regulation of translational initiation during cellular responses to stress, Prog. Nucleic Acid Res. Mol. Biol. 58 (1998) 79-125.
14. A. Bertolotti, Y. Zang, L.M. Hendershot, H.P. Harding, D. Ron, Dynamic interaction of BiP and ER stress transducers in the unfolded protein response, Nat. Cell. Biol. 2 (2000) 326-332.
15. Y. Shi et al., Identification and characterization of pancreatic eukaryotic initiation factor 2 α-subunit kinase, PEK, involved in translational control, Mol. Cell Biol. 18 (1998) 7499-7509.
16. C.R. Prostko, M.A. Brostrom, C.O. Brostrom, Reversible phosphorylation of eukaryotic initiation factor 2α in response to endoplasmic reticular signaling, Mol. Cell. Biochem. 127-128 (1993) 255-256.
17. H.P. Harding, Y. Zhang, D. Ron, Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase, Nature 397 (1999) 21.
18. T. Katayama, K. Imaizumi, N. Sato, K. Miyoshi, T. Kudo, et al., Presenilin-1 mutations downregulate the signaling pathway of the unfolded protein response, Nat. Cell. Biol. 1 (1999) 479-485.
19. Y. Nakano, G. Kondoh, T. Kudo, K. Imaizumi, M. Kato, J.I. Miyazaki, M. Tohyama, J. Takeda, M. Takeda, Accumulation of murine amyloid β42 with a gene-dosage dependent manner in PS1'knock-in' mice, Eur. J. Neurosci. 11 (1999) 2577-2581.
20. T. Katayama, K. Imaizumi, A. Honda, T. Yoneda, T. Kudo, et al., Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations, J. Biol. Chem. 16 (2001) 43446-43454.
21. H.P. Harding, I. Novoa, Y. Zhang, H. Zeng, M. Schapira, D. Ron, Regulated translation initiation controls stress-induced gene expression in mammalian cells, Mol. Cell. 6 (2000) 1099-1108.
22. H.P. Harding, Y. Zhang, A. Bertolotti, H. Zeng, D. Ron, PERK is essential for translational regulation and cell survival during the unfolded protein response, Mol. Cell. 5 (2000) 897-904.
23. J.P. Tur, S. Froelich, G. Prihar, R. Crook, M. Baker, et al., A mutation in Alzheimer's disease destroying a splice acceptor site in the presenilin-1 gene, Neuroreport 7 (1995) 297-301.
24. Q. Guo, B.L. Sopher, K. Furukawa, D.G. Pham, N. Robinson, et al., Alzheimer's Presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid β-peptide: involvement of calcium and oxyradicals, J. Neurosci. 1 (1997) 4212-4222.
25. Nazneen, N. Dewji, S.J. Singer, The seven-transmembrane spanning topography of Alzheimer's disease-related presenilin proteins in the plasma membranes of cultured cells, Proc. Natl. Acad. Sci. USA 94 (1997) 14025-14030.
26. C. Hammond, A. Helenius, Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus, J. Cell Biol. 126 (1994) 41-52.
27. D.G. Cook, M.S. Forman, J.C. Sung, S. Leight, D.L. Kolson, T.I. Watsubo, V.M. Lee, R.W. Doms, Alzheimer's Aβ(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells, Nat. Med. 3 (1997) 1021-1023.