Evidence that the COOH terminus of human presenilin 1 is located in extracytoplasmic space

American Journal of Physiology - Cell Physiology

Volumn 289, Issue 3 58-3, 2005, Pages

  Oh, Young S ^a,b   Turner, R James ^a  

^a NATIONAL INSTITUTE OF DENTAL AND CRANIOFACIAL RESEARCH   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

amyloid; secretase; Alzheimer's disease; Intramembranous protease; Transmembrane topology

Indexed keywords

AMINO ACID; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE; MEMBRANE PROTEIN; PRESENILIN 1;

ALPHA HELIX; ALZHEIMER DISEASE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EMBRYO; GENETIC LINKAGE; HUMAN; HUMAN CELL; MEMBRANE STRUCTURE; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

AMINO ACID SEQUENCE; CELL LINE; ENDOPEPTIDASE K; GENES, REPORTER; GLYCOSYLATION; HUMANS; HYDROPHOBICITY; KIDNEY; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PRESENILIN-1; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 23944511109     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.00636.2004     Document Type: Article

References (30)

1. Annaert W and De Strooper B. A cell biological perspective on Alzheimer's disease. Annu Rev Cell Dev Biol 18: 25-51, 2002.
2. Annaert WG, Esselens C, Baert V, Boeve C, Snellings G, Cupers P, Craessaerts K, and De Strooper B. Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins. Neuron 32: 579-589, 2001.
3. Annaert WG, Levesque L, Craessaerts K, Dierinck I, Snellings G, Westaway D, George-Hyslop PS, Cordell B, Fraser P, and De SB. Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-Golgi compartments of hippocampal neurons. J Cell Biol 147: 277-294, 1999.
4. Das P, Howard V, Loosbrock N, Dickson D, Murphy MP, and Golde TE. Amyloid-β immunization effectively reduces amyloid deposition in FcRγ-/- knock-out mice. J Neurosci 23: 8532-8538, 2003.
5. De Strooper B, Beullens M, Contreras B, Levesque L, Craessaerts K, Cordell B, Moechars D, Bollen M, Fraser P, George-Hyslop PS, and Van Leuven F. Phosphorylation, subcellular localization, and membrane orientation of the Alzheimer's disease-associated presenilins. J Biol Chem 272: 3590-3598, 1997.
6. Dewji NN and Singer SJ. The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells. Proc Natl Acad Sci USA 94: 14025-14030, 1997.
7. Dewji NN, Valdez D, and Singer SJ. The presenilins turned inside out: implications for their structures and functions. Proc Natl Acad Sci USA 101: 1057-1062, 2004.
8. Doan A, Thinakaran G, Borchelt DR, Slunt HH, Ratovitsky T, Podlisny M, Selkoe DJ, Seeger M, Gandy SE, Price DL, and Sisodia SS. Protein topology of presenilin 1. Neuron 17: 1023-1030, 1996.
9. 2+ channel TRPC1. J Biol Chem 279: 12242-12248, 2004.
10. Dohke Y and Turner RJ. Evidence that the transmembrane biogenesis of aquaporin 1 is cotranslational in intact mammalian cells. J Biol Chem 277: 15215-15219, 2002.
11. Donoviel DB, Hadjantonakis AK, Ikeda M, Zheng H, Hyslop PS, and Bernstein A. Mice lacking both presenilin genes exhibit early embryonic patterning defects. Genes Dev 13: 2801-2810, 1999.
12. Feramisco JD, Goldstein JL, and Brown MS. Membrane topology of human insig-1, a protein regulator of lipid synthesis. J Biol Chem 279: 8487-8496, 2004.
13. Friedmann E, Lemberg MK, Weihofen A, Dev KK, Dengler U, Rovelli G, and Martoglio B. Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins. J Biol Chem 279: 50790-50798, 2004.
14. Kim J and Schekman R. The ins and outs of presenilin 1 membrane topology. Proc Natl Acad Sci USA 101: 905-906, 2004.
15. Kim SH, Lah JJ, Thinakaran G, Levey A, and Sisodia SS. Subcellular localization of presenilins: association with a unique membrane pool in cultured cells. Neurobiol Dis 7: 99-117, 2000.
16. Lau KF, Howlett DR, Kesavapany S, Standen CL, Dingwall C, McLoughlin DM, and Miller CC. Cyclin-dependent kinase-5/p35 phosphorylates presenilin 1 to regulate carboxy-terminal fragment stability. Mol Cell Neurosci 20: 13-20, 2002.
17. Lehmann S, Chiesa R, and Harris DA. Evidence for a six-transmembrane domain structure of presenilin 1. J Biol Chem 272: 12047-12051, 1997.
18. Li X and Greenwald I. Membrane topology of the C. elegans SEL-12 presenilin. Neuron 17: 1015-1021, 1996.
19. Li X and Greenwald I. Additional evidence for an eight-transmembrane- domain topology for Caenorhabditis elegans and human presenilins. Proc Natl Acad Sci USA 95: 7109-7114, 1998.
20. Luo WJ, Wang H, Li H, Kim BS, Shah S, Lee HJ, Thinakaran G, Kim TW, Yu G, and Xu H. PEN-2 and APH-1 coordinately regulate proteolytic processing of presenilin 1. J Biol Chem 278: 7850-7854, 2003.
21. Nakai T, Yamasaki A, Sakaguchi M, Kosaka K, Mihara K, Amaya Y, and Miura S. Membrane topology of Alzheimer's disease-related presenilin 1. Evidence for the existence of a molecular species with a seven membrane-spanning and one membrane-embedded structure. J Biol Chem 274: 23647-23658, 1999.
22. Podlisny MB, Citron M, Amarante P, Sherrington R, Xia W, Zhang J, Diehl T, Levesque G, Fraser P, Haass C, Koo EH, Seubert P, St. George-Hyslop P, Teplow DB, and Selkoe DJ. Presenilin proteins undergo heterogeneous endoproteolysis between Thr291 and Ala299 and occur as stable N- and C-terminal fragments in normal and Alzheimer brain tissue. Neurobiol Dis 3: 325-337, 1997.
23. Schwarzman AL, Singh N, Tsiper M, Gregori L, Dranovsky A, Vitek MP, Glabe CG, St. George-Hyslop PH, and Goldgaber D. Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix. Proc Natl Acad Sci USA 96: 7932-7937, 1999.
24. Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81: 741-766, 2001.
25. Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, and Holman K. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375: 754-760, 1995.
26. Takasugi N, Tomita T, Hayashi I, Tsuruoka M, Niimura M, Takahashi Y, Thinakaran G, and Iwatsubo T. The role of presenilin cofactors in the γ-secretase complex. Nature 422: 438-441, 2003.
27. Van GG and Annaert W. Amyloid, presenilins, and Alzheimer's disease. Neuroscientist 9: 117-126, 2003.
28. Walter J, Capell A, Grunberg J, Pesold B, Schindzielorz A, Prior R, Podlisny MB, Fraser P, Hyslop PS, Selkoe DJ, and Haass C. The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. Mol Med 2: 673-691, 1996.
29. Xia X, Wang P, Sun X, Soriano S, Shum WK, Yamaguchi H, Trumbauer ME, Takashima A, Koo EH, and Zheng H. The aspartate-257 of presenilin 1 is indispensable for mouse development and production of β-amyloid peptides through β-catenin-independent mechanisms. Proc Natl Acad Sci USA 99: 8760-8765, 2002.
30. Zhang Z, Nadeau P, Song W, Donoviel D, Yuan M, Bernstein A, and Yankner BA. Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nat Cell Biol 2: 463-465, 2000.