Cleavage of amyloid precursor protein by an archaeal presenilin homologue PSH

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 11, 2015, Pages 3344-3349

  Dang, Shangyu ^a,b   Wu, Shenjie ^a,b   Wang, Jiawei ^c   Li, Hongbo ^a,b   Huang, Min ^d   Hea, Wei ^a,b   Li, Yue Ming ^e   Wong, Catherine C L ^d   Shi, Yigong ^a,b  

^a Tsinghua University   (China)

^b Tsinghua University   (China)

^c Tsinghua University   (China)

^d INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^e MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

Alzheimer's disease; Beta amyloid peptide; Gamma secretase; Intramembrane protease; PSH

Indexed keywords

AMYLOID BETA PROTEIN[1-38]; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; ASPARTIC ACID; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; PRESENILIN; PRESENILIN HOMOLOGUE PSH; PROTEIN INHIBITOR; PROTEINASE; UNCLASSIFIED DRUG; SECRETASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; IN VITRO STUDY; MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; AMINO ACID SEQUENCE; ARCHAEON; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY;

ARCHAEA;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; ARCHAEA; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PRESENILINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84925437392     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1502150112     Document Type: Article

References (38)

1. De Strooper B, et al. (1998) Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391(6665):387-390.
2. Selkoe DJ, Wolfe MS (2007) Presenilin: Running with scissors in the membrane. Cell 131(2):215-221.
3. De Strooper B, Iwatsubo T, Wolfe MS (2012) Presenilins and γ-secretase: Structure, function, and role Alzheimer Disease. Cold Spring Harb Perspect Med 2(1):a006304.
4. Morishima-Kawashima M (2014) Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase. Front Physiol 5:463.
5. Goate A, Hardy J (2012) Twenty years of Alzheimer's disease-causing mutations. J Neurochem 120(Suppl 1):3-8.
6. Crump CJ, Johnson DS, Li YM (2013) Development and mechanism of γ-secretase modulators for Alzheimer's disease. Biochemistry 52(19):3197-3216.
7. Lu P, et al. (2014) Three-dimensional structure of human aγ-secretase. Nature 512(7513):166-170.
8. Xie T, et al. (2014) Crystal structure of the γ-secretase component nicastrin. Proc Natl Acad Sci USA 111(37):13349-13354.
9. Torres-Arancivia C, et al. (2010) Identification of an archaeal presenilin-like intramembrane protease. PLoS ONE 5(9):e13072.
10. Li X, et al. (2013) Structure of a presenilin family intramembrane aspartate protease. Nature 493(7430):56-61.
11. Acx H, et al. (2014) Signature amyloid β profiles are produced by different γ-secretase complexes. J Biol Chem 289(7):4346-4355.
12. Kornilova AY, Das C, Wolfe MS (2003) Differential effects of inhibitors on the gammasecretase complex. Mechanistic implications. J Biol Chem 278(19):16470-16473.
13. Bielefeld-Sevigny M (2009) AlphaLISA immunoassay platform- the "no-wash" high-throughput alternative to ELISA. Assay Drug Dev Technol 7(1):90-92.
14. Chau DM, Crump CJ, Villa JC, Scheinberg DA, Li YM (2012) Familial Alzheimer disease presenilin-1 mutations alter the active site conformation of γ-secretase. J Biol Chem 287(21):17288-17296.
15. Wang H, Nefzi A, Fields GB, Lakshmana MK, Minond D (2014) AlphaLISA-based highthroughput screening assay to measure levels of soluble amyloid precursor protein α. Anal Biochem 459:24-30.
16. Yu G, et al. (2000) Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing. Nature 407(6800):48-54.
17. Shah S, et al. (2005) Nicastrin functions as a gamma-secretase-substrate receptor. Cell 122(3):435-447.
18. Dries DR, et al. (2009) Glu-333 of nicastrin directly participates in gamma-secretase activity. J Biol Chem 284(43):29714-29724.
19. Goo JS, et al. (2013) Nicastrin overexpression in transgenic mice induces aberrant behavior and APP processing. Mol Neurobiol 48(1):232-243.
20. Qi Y, Morishima-Kawashima M, Sato T, Mitsumori R, Ihara Y (2003) Distinct mechanisms by mutant presenilin 1 and 2 leading to increased intracellular levels of amyloid beta-protein 42 in Chinese hamster ovary cells. Biochemistry 42(4):1042-1052.
21. Walker ES, Martinez M, Brunkan AL, Goate A (2005) Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Abeta 42/40 ratios. J Neurochem 92(2):294-301.
22. Bentahir M, et al. (2006) Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms. J Neurochem 96(3):732-742.
23. Wolfe MS (2013) Toward the structure of presenilin/γ-secretase and presenilin homologs. Biochim Biophys Acta 1828(12):2886-2897.
24. Kretner B, et al. (2011) Attenuated Abeta42 responses to low potency gamma-secretase modulators can be overcome for many pathogenic presenilin mutants by second-generation compounds. J Biol Chem 286(17):15240-15251.
25. Borgegard T, et al. (2012) First and second generation γ-secretase modulators (GSMs) modulate amyloid-β (Aβ) peptide production through different mechanisms. J Biol Chem 287(15):11810-11819.
26. Golde TE, Koo EH, Felsenstein KM, Osborne BA, Miele L (2013) γ-Secretase inhibitors and modulators. Biochim Biophys Acta 1828(12):2898-2907.
27. Pozdnyakov N, et al. (2013) γ-Secretase modulator (GSM) photoaffinity probes reveal distinct allosteric binding sites on presenilin. J Biol Chem 288(14):9710-9720.
28. Ataka S, et al. (2004) A novel presenilin-1 mutation (Leu85Pro) in early-onset Alzheimer disease with spastic paraparesis. Arch Neurol 61(11):1773-1776.
29. Sodeyama N, et al. (2001) Very early onset Alzheimer's disease with spastic paraparesis associated with a novel presenilin 1 mutation (Phe237Ile). J Neurol Neurosurg Psychiatry 71(4):556-557.
30. Shrimpton AE, et al. (2007) A presenilin 1 mutation (L420R) in a family with early onset Alzheimer disease, seizures and cotton wool plaques, but not spastic paraparesis. Neuropathology 27(3):228-232.
31. Chun J, Yin YI, Yang G, Tarassishin L, Li YM (2004) Stereoselective synthesis of photoreactive peptidomimetic gamma-secretase inhibitors. J Org Chem 69(21):7344-7347.
32. Crump CJ, et al. (2011) Piperidine acetic acid based γ-secretase modulators directly bind to presenilin-1. ACS Chem Neurosci 2(12):705-710.
33. Fernandez MA, Klutkowski JA, Freret T, Wolfe MS (2014) Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ. J Biol Chem 289(45):31043-31052.
34. Saito T, et al. (2011) Potent amyloidogenicity and pathogenicity of Aβ43. Nat Neurosci 14(8):1023-1032.
35. Chávez-Gutiérrez L, et al. (2012) The mechanism of γ-secretase dysfunction in familial Alzheimer disease. EMBO J 31(10):2261-2274.
36. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
37. Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50(Pt 5):760-763.
38. Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58(Pt 11):1948-1954.