Alzheimer disease γ-secretase: A complex story of GxGD-type presenilin proteases

Trends in Cell Biology

Volumn 12, Issue 12, 2002, Pages 556-562

  Haass, Christian ^a   Steiner, Harald ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC PROTEINASE; GAMMA SECRETASE; NICASTRIN; PRESENILIN 1; PRESENILIN 2; PROTEINASE; MEMBRANE PROTEIN; MULTIENZYME COMPLEX; SECRETASE;

ALZHEIMER DISEASE; ENZYME ACTIVITY; HUMAN; MOLECULAR RECOGNITION; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; PROBABILITY; PROTEIN DEGRADATION; PROTEIN STABILITY; PROTEIN TARGETING; REVIEW; ANIMAL; CELL MEMBRANE; ENZYMOLOGY; METABOLISM;

ALZHEIMER DISEASE; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; ASPARTIC ENDOPEPTIDASES; CELL MEMBRANE; ENDOPEPTIDASES; MEMBRANE PROTEINS; MULTIENZYME COMPLEXES; PRESENILIN-1;

EID: 0036898485     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)02394-2     Document Type: Review

References (52)

1. Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
2. Steiner H., Haass C. Intramembrane proteolysis by presenilins. Nat. Rev. Mol. Cell Biol. 1:2000;217-224.
3. Herreman A., et al. Presenilin 2 deficiency causes a mild pulmonary phenotype and no changes in amyloid precursor protein processing but enhances the embryonic lethal phenotype of presenilin 1 deficiency. Proc. Natl. Acad. Sci. U. S. A. 96:1999;11872-11877.
4. Herreman A., et al. Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells. Nat. Cell Biol. 2:2000;461-462.
5. Zhang Z., et al. Presenilins are required for γ-secretase cleavage of βAPP and transmembrane cleavage of Notch-1. Nat. Cell Biol. 2:2000;463-465.
6. De Strooper B., et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature. 391:1998;387-390.
7. Naruse S., et al. Effects of PS1 deficiency on membrane protein trafficking in neurons. Neuron. 21:1998;1213-1221.
8. Wolfe M.S., et al. Are presenilins intramembrane-cleaving proteases? Implications for the molecular mechanism of Alzheimer's disease. Biochemistry. 38:1999;11223-11230.
9. Wolfe M.S., et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature. 398:1999;513-517.
10. Steiner H., et al. A loss of function mutation of presenilin-2 interferes with amyloid β-peptide production and Notch signaling. J. Biol. Chem. 274:1999;28669-28673.
11. Thinakaran G., et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron. 17:1996;181-190.
12. Li Y.M., et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature. 405:2000;689-694.
13. Esler W.P., et al. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nat. Cell Biol. 2:2000;428-433.
14. Beher D., et al. Pharmacological knock-down of the presenilin 1 heterodimer by a novel γ-secretase inhibitor: implications for presenilin biology. J. Biol. Chem. 276:2001;45394-45402.
15. Steiner H., et al. Glycine 384 is required for presenilin-1 function and is conserved in polytopic bacterial aspartyl proteases. Nat. Cell Biol. 2:2000;848-851.
16. LaPointe C.F., Taylor R.K. The type 4 prepilin peptidases comprise a novel family of aspartic acid proteases. J. Biol. Chem. 275:2000;1502-1510.
17. Weihofen A., et al. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science. 296:2002;2215-2218.
18. Ponting C.P., et al. Identification of a novel family of presenilin homologues. Hum. Mol. Genet. 11:2002;1037-1044.
19. 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. 273:1998;3205-3211.
20. Yu G., et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin. J. Biol. Chem. 273:1998;16470-16475.
21. Yu G., et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature. 407:2000;48-54.
22. Edbauer D., et al. Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation. Proc. Natl. Acad. Sci. U. S. A. 99:2002;8666-8671.
23. 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. 3:2002;85-97.
24. Hu Y., et al. Nicastrin is required for γ-secretase cleavage of the Drosophila Notch receptor. Dev. Cell. 2:2002;69-78.
25. Leem J.Y., et al. Presenilin 1 is required for maturation and cell surface accumulation of nicastrin. J. Biol. Chem. 277:2002;19236-19240.
26. Goutte C., et al. APH-1 is a multipass membrane protein essential for the Notch signaling pathway in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. U. S. A. 99:2002;775-779.
27. Goutte C., et al. aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling. Development. 127:2000;2481-2492.
28. 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. 277:2002;39062-39065.
29. Thinakaran G., et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272:1997;28415-28422.
30. Mumm J.S., Kopan R. Notch signaling: from the outside in. Dev. Biol. 228:2000;151-165.
31. Levitan D., Greenwald I. Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene. Nature. 377:1995;351-354.
32. Shen J., et al. Skeletal and CNS defects in Presenilin-1-deficient mice. Cell. 89:1997;629-639.
33. Wong P.C., et al. Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm. Nature. 387:1997;288-292.
34. Donoviel D.B., et al. Mice lacking both presenilin genes exhibit early embryonic patterning defects. Genes Dev. 13:1999;2801-2810.
35. Schroeter E.H., et al. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature. 393:1998;382-386.
36. De Strooper B., et al. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature. 398:1999;518-522.
37. Lopez-Schier H., Johnston D.S. Drosophila nicastrin is essential for the intramembraneous cleavage of Notch. Dev. Cell. 2:2002;79-89.
38. Chung H.-M., Struhl G. Nicastrin is required for presenilin-mediated transmembrane cleavage in Drosophila. Nat. Cell Biol. 3:2001;1129-1132.
39. Mizutani T., et al. Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members. Proc. Natl. Acad. Sci. U. S. A. 98:2001;9026-9031.
40. Saxena M.T., et al. Murine Notch homologs (N1-4) undergo presenilin-dependent proteolysis. J. Biol. Chem. 276:2001;40268-40273.
41. Ni C.Y., et al. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science. 294:2001;2179-2181.
42. Lee H.J., et al. Presenilin-dependent γ-secretase-like intramembrane cleavage of ErbB4. J. Biol. Chem. 277:2002;6318-6323.
43. Marambaud P., et al. A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 21:2002;1948-1956.
44. Lammich, S. et al. (2002) Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Aβ-like peptide. J. Biol. Chem. 10.1074/jbc.M206872200 (http://www.jbc.org).
45. Ebinu J.O., Yankner B.A. A RIP tide in neuronal signal transduction. Neuron. 34:2002;499-502.
46. Cao X., Südhof T.C. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science. 293:2001;115-120.
47. Baek S.H., et al. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-κB and β-amyloid precursor protein. Cell. 110:2002;55-67.
48. Sastre M., et al. Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. 2:2001;835-841.
49. Gu Y., et al. Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J. Biol. Chem. 276:2001;35235-35238.
50. Yu C., et al. Characterization of a presenilin-mediated APP carboxyl terminal fragment CTFγ: evidence for distinct mechanisms involved in γ-secretase processing of the APP and Notch1 transmembrane domains. J. Biol. Chem. 276:2001;43756-43760.
51. Weidemann A., et al. A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry. 41:2002;2825-2835.
52. Okochi M., et al. Presenilins mediate a dual intramembraneous γ-secretase cleavage of Notch-1. EMBO J. 21:2002;5408-5416.