The role of presenilin cofactors in the γ-secratase complex

Nature

Volumn 422, Issue 6930, 2003, Pages 438-441

  Takasugi, Nobumasa ^a   Tomita, Taisuke ^a   Hayashi, Ikuo ^a   Tsuruoka, Makiko ^a   Niimura, Manabu ^a   Takahashi, Yasuko ^a   Thinakaran, Gopal ^b   Iwatsubo, Takeshi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; DISEASES; ENZYMES; GENES; PROTEINS; RNA;

PRECURSOR PROTEINS;

GENETIC ENGINEERING;

DROSOPHILA PROTEIN; GAMMA SECRETASE; MEMBRANE PROTEIN; NICASTRIN; PRESENILIN 1; RNA;

MEDICINE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DROSOPHILA; ENHANCER REGION; FETUS; GENE DELETION; HELA CELL; HUMAN; HUMAN CELL; MAMMAL CELL; MOUSE; NERVE CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN STABILITY;

ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; ASPARTIC ENDOPEPTIDASES; CELL LINE; CELLS, CULTURED; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; ENDOPEPTIDASES; HELA CELLS; HUMANS; MACROMOLECULAR SUBSTANCES; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; NEURONS; PRESENILIN-1; PROTEIN PROCESSING, POST-TRANSLATIONAL; RNA INTERFERENCE;

ANIMALIA; MAMMALIA;

EID: 0037468759     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01506     Document Type: Article

References (28)

1. De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
2. De Strooper, B. et al. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
3. Duff, K. et al. Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1. Nature 383, 710-713 (1996).
4. Borchelt, D. R. et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 17, 1005-1013 (1996).
5. Citron, M. et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice. Nature Med. 3, 67-72 (1997).
6. Tomita, T. et al. The presenilin 2 mutation (N1411) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid β protein ending at the 42nd (or 43rd) residue. Proc. Natl Acad. Sci. USA 94, 2025-2030 (1997).
7. Ratovitski, T. et al. Endoproteolytic processing and stabilization of wild-type and mutant presenilin. J. Biol. Chem. 272, 24536-24541 (1997).
8. Thinakaran, G. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28415-28422 (1997).
9. Capell, A. et al. The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100-150-kDa molecular mass complex. J. Biol. Chem. 273, 3205-3211 (1998).
10. Tomita, T. et al. The first proline of PALP motif at the C terminus of presenilins is obligatory for stabilization, complex formation and γ-secretase activities of presenilins. J. Biol. Chem. 276, 33273-33281 (2001).
11. Takasugi, N. et al. The mechanism of γ-secretase activities through high molecular weight complex formation of presenilins is conserved in Drosophila melanogaster and mammals. J. Biol. Chem. 277, 50198-50205 (2002).
12. Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48-54 (2000).
13. Hu, Y., Ye, Y. & Fortini, M. E. Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor. Dev. Cell 2, 69-78 (2002).
14. Edbauer, D., Winkler, E., Haass, C. & Steiner, H. Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl Acad. Sci. USA 99, 8666-8671 (2002).
15. Goutte, C., Tsunozaki, M., Hale, V. A. & Priess, J. R. APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl Acad. Sci. USA 99, 775-779 (2002).
16. Francis, R. et al. aph-1 and pen-2 are required for notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
17. Lee, S. F. et al. Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-β precursor protein and notch. J. Biol. Chem. 277, 45013-45019 (2002).
18. Gu, Y. et al. APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin-nicastrin complexes. J. Biol. Chem. 278, 7374-7380 (2003).
19. Steiner, H. et al. PEN-2 is an integral component of the γ-secretase complex required for coordinated expression of presenilin and nicastrin. J. Biol. Chem. 277, 39062-39065 (2002).
20. Ui, K. et al. Newly established cell lines from Drosophila larval CNS express neural specific characters. In Vitro Cell. Dev. Biol. Anim. 30A, 209-216 (1994).
21. Elbasbir, S. M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498 (2001).
22. Fortini, M. E. γ-secretase-mediated proteolysis in cell-surface-receptor signalling. Nature Rev. Mol. Cell. Biol. 3, 673-684 (2002).
23. Urban, S. & Freeman, M. Intramembrane proteolysis controls diverse signalling pathways throughout evolution. Curr. Opin. Genet. Dev. 12, 512-518 (2002).
24. Fukumoto, H. et al. Primary cultures of neuronal and non-neuronal rat brain cells secrete similar proportions of amyloid β peptides ending at Aβ40 and Aβ42. Neuroreport 10, 2965-2969 (1999).
25. Thinakaran, G. et al. Stable association of presenilin derivatives and absence of presenilin interactions with APP. Neurobiol. Dis. 4, 438-453 (1998).
26. Morohashi, Y. et al. Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4. J. Biol. Chem. 277, 14965-14975 (2002).
27. Suzuki, N. et al. An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (βAPP717) mutants. Science 264, 1336-1340 (1994).
28. Iwatsubo, T. et al. Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: evidence that an initially deposited species is Aβ42(43). Neuron 13, 45-53 (1994).