Defining the minimum substrate and charge recognition model of gamma-secretase

Acta Pharmacologica Sinica

Volumn 38, Issue 10, 2017, Pages 1412-1424

  Yan, Yan ^a,b,c   Xu, Ting Hai ^a,b,c   Melcher, Karsten ^b   Xu, H Eric ^a,b  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b VAN ANDEL RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; NOTCH RECEPTOR; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); AMYLOID BETA-PROTEIN PRECURSOR C-TERMINAL FRAGMENT BETA, HUMAN; PEPTIDE FRAGMENT; SECRETASE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; AMYLOID PLAQUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; HUMAN; HUMAN CELL; INTRACELLULAR MEMBRANE; LUMINESCENCE; PROTEIN CLEAVAGE; PROTEIN ISOLATION; PROTEIN SECONDARY STRUCTURE; SUBSTRATE CONCENTRATION; WESTERN BLOTTING; CELL CULTURE; ENZYME SPECIFICITY; METABOLISM; PATHOPHYSIOLOGY;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; CELLS, CULTURED; HUMANS; PEPTIDE FRAGMENTS; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; RECEPTORS, NOTCH; SUBSTRATE SPECIFICITY;

EID: 85029751403     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2017.35     Document Type: Article

References (40)

1. Zheng H, Koo EH. Biology and pathophysiology of the amyloid precursor protein. Mol Neurodegener 2011; 6: 27.
2. Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci 1997; 20: 154-9.
3. Nunan J, Small DH. Regulation of APP cleavage by alpha-, beta-and gamma-secretases. FEBS Lett 2000; 483: 6-10.
4. Jiang S, Li Y, Zhang X, Bu G, Xu H, Zhang YW. Trafficking regulation of proteins in Alzheimer's disease. Mol Neurodegener 2014; 9:6.
5. Zhang S, Zhang M, Cai F, Song W. Biological function of Presenilin and its role in AD pathogenesis. Transl Neurodegener 2013; 2: 15.
6. Morishima-Kawashima M, Ihara Y. Alzheimer's disease: beta-Amyloid protein and tau. J Neurosci Res 2002; 70: 392-401.
7. Zhang YW, Thompson R, Zhang H, Xu H. APP processing in Alzheimer's disease. Mol Brain 2011; 4:3.
8. Takami M, Nagashima Y, Sano Y, Ishihara S, Morishima-Kawashima M, Funamoto S, et al. gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of betacarboxyl terminal fragment. J Neurosci 2009; 29: 13042-52.
9. Shih IeM, Wang TL. Notch signaling, gamma-secretase inhibitors, and cancer therapy. Cancer Res 2007; 67: 1879-82.
10. Borggrefe T, Oswald F. The Notch signaling pathway: transcriptional regulation at Notch target genes. Cell Mol Life Sci 2009; 66: 1631-46.
11. Fiuza UM, Arias AM. Cell and molecular biology of Notch. J Endocrinol 2007; 194: 459-74.
12. Edbauer D, Winkler E, Regula JT, Pesold B, Steiner H, Haass C. Reconstitution of gamma-secretase activity. Nat Cell Biol 2003; 5: 486-8.
13. De Strooper B. Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex. Neuron 2003; 38: 9-12.
14. Takasugi N, Tomita T, Hayashi I, Tsuruoka M, Niimura M, Takahashi Y, et al. The role of presenilin cofactors in the gamma-secretase complex. Nature 2003; 422: 438-41.
15. De Strooper B, Vassar R, Golde T. The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat Rev Neurol 2010; 6: 99-107.
16. De Strooper B, Iwatsubo T, Wolfe MS. Presenilins and gammasecretase: structure, function, and role in Alzheimer disease. Cold Spring Harb Perspect Med 2012; 2: a006304.
17. Chen F, Hasegawa H, Schmitt-Ulms G, Kawarai T, Bohm C, Katayama T, et al. TMP21 is a presenilin complex component that modulates gamma-secretase but not epsilon-secretase activity. Nature 2006; 440: 1208-12.
18. LaVoie MJ, Fraering PC, Ostaszewski BL, Ye W, Kimberly WT, Wolfe MS, et al. Assembly of the gamma-secretase complex involves early formation of an intermediate subcomplex of Aph-1 and nicastrin. J Biol Chem 2003; 278: 37213-22.
19. Lee SF, Shah S, Yu C, Wigley WC, Li H, Lim M, et al. A conserved GXXXG motif in APH-1 is critical for assembly and activity of the gamma-secretase complex. J Biol Chem 2004; 279: 4144-52.
20. Watanabe N, Tomita T, Sato C, Kitamura T, Morohashi Y, Iwatsubo T. Pen-2 is incorporated into the gamma-secretase complex through binding to transmembrane domain 4 of presenilin 1. J Biol Chem 2005; 280: 41967-75.
21. Bai XC, Yan C, Yang G, Lu P, Ma D, Sun L, et al. An atomic structure of human gamma-secretase. Nature 2015; 525: 212-7.
22. Shah S, Lee SF, Tabuchi K, Hao YH, Yu C, LaPlant Q, et al. Nicastrin functions as a gamma-secretase-substrate receptor. Cell 2005; 122: 435-47.
23. Zhao G, Liu Z, Ilagan MX, Kopan R. Gamma-secretase composed of PS1/Pen2/Aph1a can cleave notch and amyloid precursor protein in the absence of nicastrin. J Neurosci 2010; 30: 1648-56.
24. Li S, Zhang W, Han W. Initial substrate binding of gamma-secretase: the role of substrate flexibility. ACS Chem Neurosci 2017. doi: 10.1021/acschemneuro.6b00425.
25. Bolduc DM, Montagna DR, Seghers MC, Wolfe MS, Selkoe DJ. The amyloid-beta forming tripeptide cleavage mechanism of gammasecretase. Elife 2016; 5. pii: e17578.
26. Fukumori A, Steiner H. Substrate recruitment of gamma-secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping. EMBO J 2016; 35: 1628-43.
27. Barnea G, Strapps W, Herrada G, Berman Y, Ong J, Kloss B, et al. The genetic design of signaling cascades to record receptor activation. Proc Natl Acad Sci U S A 2008; 105: 64-9.
28. Xu TH, Yan Y, Kang Y, Jiang Y, Melcher K, Xu HE. Alzheimer's diseaseassociated mutations increase amyloid precursor protein resistance to gamma-secretase cleavage and the Abeta42/Abeta40 ratio. Cell Discov 2016; 2: 16026.
29. LaFerla FM, Green KN, Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 2007; 8: 499-509.
30. Haapasalo A, Kovacs DM. The many substrates of presenilin/gammasecretase. J Alzheimers Dis 2011; 25: 3-28.
31. Funamoto S, Sasaki T, Ishihara S, Nobuhara M, Nakano M, Watanabe-Takahashi M, et al. Substrate ectodomain is critical for substrate preference and inhibition of gamma-secretase. Nat Commun 2013; 4: 2529.
32. Tian Y, Bassit B, Chau D, Li YM. An APP inhibitory domain containing the Flemish mutation residue modulates gamma-secretase activity for Abeta production. Nat Struct Mol Biol 2010; 17: 151-8.
33. Suh BC, Hille B. PIP2 is a necessary cofactor for ion channel function: how and why? Annu Rev Biophys 2008; 37: 175-95.
34. McLaughlin S, Wang J, Gambhir A, Murray D. PIP2 and proteins: interactions, organization, and information flow. Annu Rev Biophys Biomol Struct 2002; 31: 151-75.
35. Landman N, Jeong SY, Shin SY, Voronov SV, Serban G, Kang MS, et al. Presenilin mutations linked to familial Alzheimer's disease cause an imbalance in phosphatidylinositol 4,5-bisphosphate metabolism. Proc Natl Acad Sci U S A 2006; 103: 19524-9.
36. Yin YI, Bassit B, Zhu L, Yang X, Wang C, Li YM. gamma-Secretase substrate concentration modulates the Abeta42/Abeta40 ratio: implications for Alzheimer disease. J Biol Chem 2007; 282: 23639-44.
37. Okochi M, Tagami S, Yanagida K, Takami M, Kodama TS, Mori K, et al. gamma-Secretase modulators and presenilin 1 mutants act differently on presenilin/gamma-secretase function to cleave Abeta42 and Abeta43. Cell Rep 2013; 3: 42-51.
38. Fernandez MA, Klutkowski JA, Freret T, Wolfe MS. Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid beta-peptides (Abeta) by gamma-secretase to increase 42-to-40-residue Abeta. J Biol Chem 2014; 289: 31043-52.
39. Haass C, Hung AY, Schlossmacher MG, Teplow DB, Selkoe DJ. beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J Biol Chem 1993; 268: 3021-4.
40. Buchan DW, Minneci F, Nugent TC, Bryson K, Jones DT. Scalable web services for the PSIPRED Protein Analysis Workbench. Nucleic Acids Res 2013; 41: W349-57.