Notch and Presenilin: A proteolytic mechanism emerges

Current Opinion in Cell Biology

Volumn 13, Issue 5, 2001, Pages 627-634

  Fortini, M E ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; MEMBRANE PROTEIN; PRESENILIN 1; PRESENILIN 2;

ALZHEIMER DISEASE; CATALYSIS; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FAMILY; PROTEIN PROCESSING; REVIEW; SIGNAL TRANSDUCTION;

EID: 0035479911     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00261-1     Document Type: Review

References (72)

1. Proteases to die for
2. The world according to hedgehog
3. Ci: A complex transducer of the Hedgehog signal
4. Signal transduction by a protease cascade
5. Notch signaling: Cell fate control and signal integration in development
6. The ins and outs of Notch signaling
7. Notch: Neurogenesis is only part of the picture
8. Structure/function studies of lin-12/Notch proteins
9. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
10. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1
11. Translating cell biology into therapeutic advances in Alzheimer's disease
12. Intramembrane proteolysis by presenilins
13. Proteolytic processing and cell biological functions of the amyloid precursor protein
14. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
15. Effects of PS1 deficiency on membrane protein trafficking in neurons
16. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
17. A loss of function mutation of Presenilin-2 interferes with amyloid β-peptide production and Notch signaling
18. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state
19. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
20. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
21. Presenilin-1 and -2 are molecular targets for γ-secretase inhibitors
22. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases
23. Presenilins, processing of β-amyloid precursor protein, and Notch signaling
24. A common enzyme connects Notch signaling and Alzheimer's disease
25. Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene
26. HOP-1, a Caenorhabditis elegans presenilin, appears to be functionally redundant with SEL-12 presenilin and to facilitate LIN-12 and GLP-1 signaling
27. Reverse genetic analysis of Caenorhabditis elegans presenilins reveals redundant but unequal roles for sel-12 and hop-1 in Notch-pathway signaling
28. Presenilin is required for activity and nuclear access of Notch in Drosophila
29. Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants
30. Drosophila presenilin is required for neuronal differentiation and affects Notch subcellular localization and signaling
31. Skeletal and CNS defects in Presenilin-1-deficient mice
32. Presenilin 1 is required for Notch1 and Dll1 expression in the paraxial mesoderm
33. Mice lacking both presenilin genes exhibit early embryonic patterning defects
34. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
35. Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of Notch
36. Proteolytic release and nuclear translocation of Notch-1 are induced by presenilin-1 and impaired by pathogenic presenilin-1 mutations
37. Lack of requirement for Presenilin1 in Notch1 signaling
38. Aspartate mutations in Presenilin and γ-secretase inhibitors both impair Notch1 proteolysis and nuclear translocation with relative preservation of Notch1 signaling
39. Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells
40. Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1
41. Presenilin-mediated transmembrane cleavage is required for Notch signal transduction in Drosophila
42. Effects of SEL-12 presenilin on LIN-12 localization and function in Caenorhabditis elegans
43. Characterization of Drosophila Presenilin and its colocalization with Notch during development
44. Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane
45. The Notch1 receptor is cleaved constitutively by a furin-like convertase
46. Calcium depletion dissociates and activates heterodimeric Notch receptors
47. Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
48. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
49. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
50. The metalloprotease-disintegrin Kuzbanian participates in Notch activation during growth and patterning of Drosophila imaginal discs
51. SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling
52. A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1
53. A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
54. Processing of the Notch ligand Delta by the metalloprotease Kuzbanian
55. Requirement for dynamin during Notch signaling in Drosophila neurogenesis
56. Ligand endocytosis drives receptor dissociation and activation in the Notch pathway
57. Requirements for Presenilin-dependent cleavage of Notch and other transmembrane domain proteins
58. γ-secretase, evidence for multiple proteolytic activities and influence of membrane position of substrate on generation of amyloid β peptides of varying length
59. Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch
60. Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch
61. 42 secretion in mammalian cells but impaired Notch/lin-12 signalling in C. elegans
62. Ligand-induced signaling in the absence of furin processing of Notch1
63. Presenilin affects Armadillo/β-catenin localization and function in Drosophila
64. Presenilin 1 negatively regulates β-catenin/T cell factor/lymphocyte enhancer factor-1 signaling independently of β-amyloid and Notch processing
65. Evidence that an IRES within the Notch2 coding region can direct expression of a nuclear form of the protein
66. aph-2 encodes a novel extracellular protein required for GLP-1-mediated signaling
67. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
68. Requirement for Presenilin 1 in facilitating Jagged 2-mediated endoproteolysis and signaling of Notch 1
69. Effect of PS1 deficiency and an APP γ-secretase inhibitor on Notch1 signaling in primary mammalian neurons
70. Notch-1 activation by familial Alzheimer's disease (FAD)-linked mutant forms of Presenilin-1
71. Nicastrin binds to membrane-tethered Notch
72. New protease inhibitors prevent γ-secretase-mediated production of Ab40/42 without affecting Notch cleavage