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Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease
Andreas Weihofen,1Kathleen Binns,2Marius K. Lemberg,1Keith Ashman,2Bruno Martoglio1*
Signal peptide peptidase (SPP) catalyzes intramembrane proteolysis
of some signal peptides after they have been cleaved froma preprotein.
In humans, SPP activity is required to generatesignal
sequence-derived human lymphocyte antigen-E epitopes thatare
recognized by the immune system, and to process hepatitisC virus core
protein. We have identified human SPP as a polytopicmembrane protein
with sequence motifs characteristic of the presenilin-typeaspartic
proteases. SPP and potential eukaryotic homologs mayrepresent another
family of aspartic proteases that promote intramembraneproteolysis to
release biologically important peptides.
1 Institute of Biochemistry, Swiss Federal
Institute of Technology (ETH), ETH-Hoenggerberg, 8093 Zürich,
Switzerland.
2 Samuel Lunenfeld Institute,
Proteomics, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada.
*
To whom correspondence should be addressed. E-mail:
bruno.martoglio{at}bc.biol.ethz.ch
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R. Pardossi-Piquard, S.-P. Yang, S. Kanemoto, Y. Gu, F. Chen, C. Bohm, J. Sevalle, T. Li, P. C. Wong, F. Checler, et al. (2009)
J. Biol. Chem.
284, 16298-16307
|Abstract »|Full Text »|PDF »
Intramembrane Proteolysis by Signal Peptide Peptidases: A Comparative Discussion of GXGD-type Aspartyl Proteases.
R. Fluhrer, H. Steiner, and C. Haass (2009)
J. Biol. Chem.
284, 13975-13979
|Abstract »|Full Text »|PDF »
Nicastrin Is Dispensable for {gamma}-Secretase Protease Activity in the Presence of Specific Presenilin Mutations.
E. Futai, S. Yagishita, and S. Ishiura (2009)
J. Biol. Chem.
284, 13013-13022
|Abstract »|Full Text »|PDF »
The Signal Peptide Peptidase Is Required for Pollen Function in Arabidopsis.
S. Han, L. Green, and D. J. Schnell (2009)
Plant Physiology
149, 1289-1301
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Substrate Requirements for SPPL2b-dependent Regulated Intramembrane Proteolysis.
Alternative Processing of Sterol Regulatory Element Binding Protein During Larval Development in Drosophila melanogaster.
K. A. Matthews, A. S. Kunte, E. Tambe-Ebot, and R. B. Rawson (2009)
Genetics
181, 119-128
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An Internal Signal Sequence Directs Intramembrane Proteolysis of a Cellular Immunoglobulin Domain Protein.
T. Robakis, B. Bak, S.-h. Lin, D. J. Bernard, and P. Scheiffele (2008)
J. Biol. Chem.
283, 36369-36376
|Abstract »|Full Text »|PDF »
Distinct Pharmacological Effects of Inhibitors of Signal Peptide Peptidase and {gamma}-Secretase.
T. Sato, K. Ananda, C. I. Cheng, E. J. Suh, S. Narayanan, and M. S. Wolfe (2008)
J. Biol. Chem.
283, 33287-33295
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Intramembrane Proteolysis of GXGD-type Aspartyl Proteases Is Slowed by a Familial Alzheimer Disease-like Mutation.
R. Fluhrer, A. Fukumori, L. Martin, G. Grammer, M. Haug-Kroper, B. Klier, E. Winkler, E. Kremmer, M. M. Condron, D. B. Teplow, et al. (2008)
J. Biol. Chem.
283, 30121-30128
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Intramembrane Processing by Signal Peptide Peptidase Regulates the Membrane Localization of Hepatitis C Virus Core Protein and Viral Propagation.
K. Okamoto, Y. Mori, Y. Komoda, T. Okamoto, M. Okochi, M. Takeda, T. Suzuki, K. Moriishi, and Y. Matsuura (2008)
J. Virol.
82, 8349-8361
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Presenilins: Members of the {gamma}-Secretase Quartets, But Part-Time Soloists Too.
Preprocalcitonin signal peptide generates a cytotoxic T lymphocyte-defined tumor epitope processed by a proteasome-independent pathway.
F. El Hage, V. Stroobant, I. Vergnon, J.-F. Baurain, H. Echchakir, V. Lazar, S. Chouaib, P. G. Coulie, and F. Mami-Chouaib (2008)
PNAS
105, 10119-10124
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Phosphoinositides Suppress {gamma}-Secretase in Both the Detergent-soluble and -insoluble States.
S. Osawa, S. Funamoto, M. Nobuhara, S. Wada-Kakuda, M. Shimojo, S. Yagishita, and Y. Ihara (2008)
J. Biol. Chem.
283, 19283-19292
|Abstract »|Full Text »|PDF »
Transmembrane Domain 9 of Presenilin Determines the Dynamic Conformation of the Catalytic Site of {gamma}-Secretase.
A. Tolia, K. Horre, and B. De Strooper (2008)
J. Biol. Chem.
283, 19793-19803
|Abstract »|Full Text »|PDF »
Maturation of Hepatitis C Virus Core Protein by Signal Peptide Peptidase Is Required for Virus Production.
P. Targett-Adams, G. Hope, S. Boulant, and J. McLauchlan (2008)
J. Biol. Chem.
283, 16850-16859
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Regulation of alternative polyadenylation by genomic imprinting.
A. J. Wood, R. Schulz, K. Woodfine, K. Koltowska, C. V. Beechey, J. Peters, D. Bourc'his, and R. J. Oakey (2008)
Genes & Dev.
22, 1141-1146
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The Signal Peptide of the Mouse Mammary Tumor Virus Rem Protein Is Released from the Endoplasmic Reticulum Membrane and Accumulates in Nucleoli.
E. Dultz, M. Hildenbeutel, B. Martoglio, J. Hochman, B. Dobberstein, and K. Kapp (2008)
J. Biol. Chem.
283, 9966-9976
|Abstract »|Full Text »|PDF »
Regulated Intramembrane Proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b.
L. Martin, R. Fluhrer, K. Reiss, E. Kremmer, P. Saftig, and C. Haass (2008)
J. Biol. Chem.
283, 1644-1652
|Abstract »|Full Text »|PDF »
Signal Peptide Peptidase and {gamma}-Secretase Share Equivalent Inhibitor Binding Pharmacology.
L. G. Iben, R. E. Olson, L. A. Balanda, S. Jayachandra, B. J. Robertson, V. Hay, J. Corradi, C. V. C. Prasad, R. Zaczek, C. F. Albright, et al. (2007)
J. Biol. Chem.
282, 36829-36836
|Abstract »|Full Text »|PDF »
Active {gamma}-Secretase Complexes Contain Only One of Each Component.
T. Sato, T. S. Diehl, S. Narayanan, S. Funamoto, Y. Ihara, B. De Strooper, H. Steiner, C. Haass, and M. S. Wolfe (2007)
J. Biol. Chem.
282, 33985-33993
|Abstract »|Full Text »|PDF »
Signal Peptide Requirements for Lymphocytic Choriomeningitis Virus Glycoprotein C Maturation and Virus Infectivity.
S. Schrempf, M. Froeschke, T. Giroglou, D. von Laer, and B. Dobberstein (2007)
J. Virol.
81, 12515-12524
|Abstract »|Full Text »|PDF »
A C-terminal Region of Signal Peptide Peptidase Defines a Functional Domain for Intramembrane Aspartic Protease Catalysis.
S. Narayanan, T. Sato, and M. S. Wolfe (2007)
J. Biol. Chem.
282, 20172-20179
|Abstract »|Full Text »|PDF »
A Plasminogen-Like Protease in Thyroid Rough Microsomes Degrades Thyroperoxidase and Thyroglobulin.
A. Giraud, P.-J. Lejeune, J. Barbaria, and B. Mallet (2007)
Endocrinology
148, 2886-2893
|Abstract »|Full Text »|PDF »
From the Cover: Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.
R. P. Baker, K. Young, L. Feng, Y. Shi, and S. Urban (2007)
PNAS
104, 8257-8262
|Abstract »|Full Text »|PDF »
Rhomboid proteins: conserved membrane proteases with divergent biological functions..
Signal Peptide Peptidase Cleavage of GB Virus B Core Protein Is Required for Productive Infection in Vivo.
P. Targett-Adams, T. Schaller, G. Hope, R. E. Lanford, S. M. Lemon, A. Martin, and J. McLauchlan (2006)
J. Biol. Chem.
281, 29221-29227
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Signal Peptide Peptidase-catalyzed Cleavage of Hepatitis C Virus Core Protein Is Dispensable for Virus Budding but Destabilizes the Viral Capsid.
C. Vauloup-Fellous, V. Pene, J. Garaud-Aunis, F. Harper, S. Bardin, Y. Suire, E. Pichard, A. Schmitt, P. Sogni, G. Pierron, et al. (2006)
J. Biol. Chem.
281, 27679-27692
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Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase.
A. C. Nyborg, T. B. Ladd, K. Jansen, T. Kukar, and T. E. Golde (2006)
FASEB J
20, 1671-1679
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C-terminal Fragment of Presenilin Is the Molecular Target of a Dipeptidic {gamma}-Secretase-specific Inhibitor DAPT (N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-S-phenylglycine t-Butyl Ester).
Y. Morohashi, T. Kan, Y. Tominari, H. Fuwa, Y. Okamura, N. Watanabe, C. Sato, H. Natsugari, T. Fukuyama, T. Iwatsubo, et al. (2006)
J. Biol. Chem.
281, 14670-14676
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Identification of the Amino Acid Residues Essential for Proteolytic Activity in an Archaeal Signal Peptide Peptidase.
R. Matsumi, H. Atomi, and T. Imanaka (2006)
J. Biol. Chem.
281, 10533-10539
|Abstract »|Full Text »|PDF »
The GxGD motif of presenilin contributes to catalytic function and substrate identification of gamma-secretase..
A. Yamasaki, S. Eimer, M. Okochi, A. Smialowska, C. Kaether, R. Baumeister, C. Haass, and H. Steiner (2006)
J. Neurosci.
26, 3821-3828
|Abstract »|Full Text »|PDF »
Core protein cleavage by signal peptide peptidase is required for hepatitis C virus-like particle assembly..
M. Ait-Goughoulte, C. Hourioux, R. Patient, S. Trassard, D. Brand, and P. Roingeard (2006)
J. Gen. Virol.
87, 855-860
|Abstract »|Full Text »|PDF »
Functional analyses of GB virus B p13 protein: Development of a recombinant GB virus B hepatitis virus with a p7 protein.
S. Takikawa, R. E. Engle, S. U. Emerson, R. H. Purcell, M. St. Claire, and J. Bukh (2006)
PNAS
103, 3345-3350
|Abstract »|Full Text »|PDF »
Core Protein of Pestiviruses Is Processed at the C Terminus by Signal Peptide Peptidase.
M. Heimann, G. R. Sosa, B. Martoglio, H.-J. Thiel, and T. Rumenapf (2006)
J. Virol.
80, 1915-1921
|Abstract »|Full Text »|PDF »
Reconstitution of {gamma}-secretase by truncated presenilin (PS) fragments revealed that PS C-terminal transmembrane domain is critical for formation of {gamma}-secretase complex.
H. Shiraishi, T. Marutani, H.-Q. Wang, Y. Maeda, Y. Kurono, A. Takashima, W. Araki, M. Nishimura, K. Yanagisawa, and H. Komano (2006)
Genes Cells
11, 83-93
|Abstract »|Full Text »|PDF »
Differential Localization and Identification of a Critical Aspartate Suggest Non-redundant Proteolytic Functions of the Presenilin Homologues SPPL2b and SPPL3.
P. Krawitz, C. Haffner, R. Fluhrer, H. Steiner, B. Schmid, and C. Haass (2005)
J. Biol. Chem.
280, 39515-39523
|Abstract »|Full Text »|PDF »
Hepatitis C Virus Core Protein Inhibits Mitochondrial Electron Transport and Increases Reactive Oxygen Species (ROS) Production.
M. Korenaga, T. Wang, Y. Li, L. A. Showalter, T. Chan, J. Sun, and S. A. Weinman (2005)
J. Biol. Chem.
280, 37481-37488
|Abstract »|Full Text »|PDF »
Signal peptide peptidase promotes the formation of hepatitis C virus non-enveloped particles and is captured on the viral membrane during assembly.
N. Majeau, V. Gagne, M. Bolduc, and D. Leclerc (2005)
J. Gen. Virol.
86, 3055-3064
|Abstract »|Full Text »|PDF »
CD74 Is a Member of the Regulated Intramembrane Proteolysis-processed Protein Family.
S. Becker-Herman, G. Arie, H. Medvedovsky, A. Kerem, and I. Shachar (2005)
Mol. Biol. Cell
16, 5061-5069
|Abstract »|Full Text »|PDF »
Drosophila Signal Peptide Peptidase Is an Essential Protease for Larval Development.
D. J. Casso, S. Tanda, B. Biehs, B. Martoglio, and T. B. Kornberg (2005)
Genetics
170, 139-148
|Abstract »|Full Text »|PDF »
The initial substrate-binding site of {gamma}-secretase is located on presenilin near the active site.
A. Y. Kornilova, F. Bihel, C. Das, and M. S. Wolfe (2005)
PNAS
102, 3230-3235
|Abstract »|Full Text »|PDF »
{gamma}-Secretase Complex Assembly within the Early Secretory Pathway.
A. Capell, D. Beher, S. Prokop, H. Steiner, C. Kaether, M. S. Shearman, and C. Haass (2005)
J. Biol. Chem.
280, 6471-6478
|Abstract »|Full Text »|PDF »
Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity.
Molecular Determinants for Subcellular Localization of Hepatitis C Virus Core Protein.
R. Suzuki, S. Sakamoto, T. Tsutsumi, A. Rikimaru, K. Tanaka, T. Shimoike, K. Moriishi, T. Iwasaki, K. Mizumoto, Y. Matsuura, et al. (2005)
J. Virol.
79, 1271-1281
|Abstract »|Full Text »|PDF »
Processing of Notch and amyloid precursor protein by {gamma}-secretase is spatially distinct.
L. Tarassishin, Y. I. Yin, B. Bassit, and Y.-M. Li (2004)
PNAS
101, 17050-17055
|Abstract »|Full Text »|PDF »
Consensus Analysis of Signal Peptide Peptidase and Homologous Human Aspartic Proteases Reveals Opposite Topology of Catalytic Domains Compared with Presenilins.
E. Friedmann, M. K. Lemberg, A. Weihofen, K. K. Dev, U. Dengler, G. Rovelli, and B. Martoglio (2004)
J. Biol. Chem.
279, 50790-50798
|Abstract »|Full Text »|PDF »
Ectodomain Shedding and Intramembrane Cleavage of Mammalian Notch Proteins Are Not Regulated through Oligomerization.
M. Vooijs, E. H. Schroeter, Y. Pan, M. Blandford, and R. Kopan (2004)
J. Biol. Chem.
279, 50864-50873
|Abstract »|Full Text »|PDF »
Membrane Binding Properties and Terminal Residues of the Mature Hepatitis C Virus Capsid Protein in Insect Cells.
T. Ogino, H. Fukuda, S. Imajoh-Ohmi, M. Kohara, and A. Nomoto (2004)
J. Virol.
78, 11766-11777
|Abstract »|Full Text »|PDF »
The Caenorhabditis elegans IMPAS gene, imp-2, is essential for development and is functionally distinct from related presenilins.
A. P. Grigorenko, Y. K. Moliaka, M. C. Soto, C. C. Mello, and E. I. Rogaev (2004)
PNAS
101, 14955-14960
|Abstract »|Full Text »|PDF »
A Signal Peptide Peptidase (SPP) Reporter Activity Assay Based on the Cleavage of Type II Membrane Protein Substrates Provides Further Evidence for an Inverted Orientation of the SPP Active Site Relative to Presenilin.
A. C. Nyborg, K. Jansen, T. B. Ladd, A. Fauq, and T. E. Golde (2004)
J. Biol. Chem.
279, 43148-43156
|Abstract »|Full Text »|PDF »
Identification of Distinct {gamma}-Secretase Complexes with Different APH-1 Variants.
K. Shirotani, D. Edbauer, S. Prokop, C. Haass, and H. Steiner (2004)
J. Biol. Chem.
279, 41340-41345
|Abstract »|Full Text »|PDF »
Co-expression of Nicastrin and Presenilin Rescues a Loss of Function Mutant of APH-1.
D. Edbauer, C. Kaether, H. Steiner, and C. Haass (2004)
J. Biol. Chem.
279, 37311-37315
|Abstract »|Full Text »|PDF »
Targeting of Hepatitis C Virus Core Protein to Mitochondria through a Novel C-Terminal Localization Motif.
B. Schwer, S. Ren, T. Pietschmann, J. Kartenbeck, K. Kaehlcke, R. Bartenschlager, T. S. B. Yen, and M. Ott (2004)
J. Virol.
78, 7958-7968
|Abstract »|Full Text »|PDF »
Intramembrane Proteolysis and Endoplasmic Reticulum Retention of Hepatitis C Virus Core Protein.
K. Okamoto, K. Moriishi, T. Miyamura, and Y. Matsuura (2004)
J. Virol.
78, 6370-6380
|Abstract »|Full Text »|PDF »
Proteomic Analysis of Cleavage Events Reveals a Dynamic Two-step Mechanism for Proteolysis of a Key Parasite Adhesive Complex.
X. W. Zhou, M. J. Blackman, S. A. Howell, and V. B. Carruthers (2004)
Mol. Cell. Proteomics
3, 565-576
|Abstract »|Full Text »|PDF »
Requirement of PEN-2 for Stabilization of the Presenilin N-/C-terminal Fragment Heterodimer within the {gamma}-Secretase Complex.
S. Prokop, K. Shirotani, D. Edbauer, C. Haass, and H. Steiner (2004)
J. Biol. Chem.
279, 23255-23261
|Abstract »|Full Text »|PDF »
The Proteolytic Processing of the Amyloid Precursor Protein Gene Family Members APLP-1 and APLP-2 Involves {alpha}-, {beta}-, {gamma}-, and {epsilon}-Like Cleavages: MODULATION OF APLP-1 PROCESSING BY N-GLYCOSYLATION.
S. Eggert, K. Paliga, P. Soba, G. Evin, C. L. Masters, A. Weidemann, and K. Beyreuther (2004)
J. Biol. Chem.
279, 18146-18156
|Abstract »|Full Text »|PDF »
Signal Peptide Peptidase Forms a Homodimer That Is Labeled by an Active Site-directed {gamma}-Secretase Inhibitor.
A. C. Nyborg, A. Y. Kornilova, K. Jansen, T. B. Ladd, M. S. Wolfe, and T. E. Golde (2004)
J. Biol. Chem.
279, 15153-15160
|Abstract »|Full Text »|PDF »
From the Cover: The presenilins turned inside out: Implications for their structures and functions.
Presenilins Mutated at Asp-257 or Asp-385 Restore Pen-2 Expression and Nicastrin Glycosylation but Remain Catalytically Inactive in the Absence of Wild Type Presenilin.
O. Nyabi, M. Bentahir, K. Horre, A. Herreman, N. Gottardi-Littell, C. Van Broeckhoven, P. Merchiers, K. Spittaels, W. Annaert, and B. De Strooper (2003)
J. Biol. Chem.
278, 43430-43436
|Abstract »|Full Text »|PDF »
Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C.
M. Froeschke, M. Basler, M. Groettrup, and B. Dobberstein (2003)
J. Biol. Chem.
278, 41914-41920
|Abstract »|Full Text »|PDF »
{gamma}-Secretase activity is dispensable for mesenchyme-to-epithelium transition but required for podocyte and proximal tubule formation in developing mouse kidney.
H.-T. Cheng, J. H. Miner, M. Lin, M. G. Tansey, K. Roth, and R. Kopan (2003)
Development
130, 5031-5042
|Abstract »|Full Text »|PDF »
Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs.
Hepatitis C Virus-Like Particle Budding: Role of the Core Protein and Importance of Its Asp111.
E. Blanchard, C. Hourioux, D. Brand, M. Ait-Goughoulte, A. Moreau, S. Trassard, P.-Y. Sizaret, F. Dubois, and P. Roingeard (2003)
J. Virol.
77, 10131-10138
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Requirement of the Proteasome for the Trimming of Signal Peptide-derived Epitopes Presented by the Nonclassical Major Histocompatibility Complex Class I Molecule HLA-E.
F. A. Bland, M. K. Lemberg, A. J. McMichael, B. Martoglio, and V. M. Braud (2003)
J. Biol. Chem.
278, 33747-33752
|Abstract »|Full Text »|PDF »
Intramembrane proteolysis by presenilin and presenilin-like proteases.
Induction of Pathogenic Sets of Genes in Macrophages and Neurons in NeuroAIDS.
E. S. Roberts, M. A. Zandonatti, D. D. Watry, L. J. Madden, S. J. Henriksen, M. A. Taffe, and H. S. Fox (2003)
Am. J. Pathol.
162, 2041-2057
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Differential Effects of Inhibitors on the gamma -Secretase Complex. MECHANISTIC IMPLICATIONS.
A. Y. Kornilova, C. Das, and M. S. Wolfe (2003)
J. Biol. Chem.
278, 16470-16473
|Abstract »|Full Text »|PDF »
Targeting Presenilin-type Aspartic Protease Signal Peptide Peptidase with gamma -Secretase Inhibitors.
A. Weihofen, M. K. Lemberg, E. Friedmann, H. Rueeger, A. Schmitz, P. Paganetti, G. Rovelli, and B. Martoglio (2003)
J. Biol. Chem.
278, 16528-16533
|Abstract »|Full Text »|PDF »
A Novel Family in Medicago truncatula Consisting of More Than 300 Nodule-Specific Genes Coding for Small, Secreted Polypeptides with Conserved Cysteine Motifs.
P. Mergaert, K. Nikovics, Z. Kelemen, N. Maunoury, D. Vaubert, A. Kondorosi, and E. Kondorosi (2003)
Plant Physiology
132, 161-173
|Abstract »|Full Text »|PDF »
Amyloid, Presenilins, and Alzheimer's Disease.
G. V. Gassen and W. Annaert (2003)
Neuroscientist
9, 117-126
|Abstract »|PDF »
{gamma}-Secretase--Intramembrane Protease with a Complex.
{gamma}-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation.
A. Herreman, G. Van Gassen, M. Bentahir, O. Nyabi, K. Craessaerts, U. Mueller, W. Annaert, and B. De Strooper (2003)
J. Cell Sci.
116, 1127-1136
|Abstract »|Full Text »|PDF »
Physiologic and Pathologic Events Mediated by Intramembranous and Juxtamembranous Proteolysis.
Familial Alzheimer Disease-linked Presenilin 1 Variants Enhance Production of Both Abeta 1-40 and Abeta 1-42 Peptides That Are Only Partially Sensitive to a Potent Aspartyl Protease Transition State Inhibitor of "gamma -Secretase".
T. Ikeuchi, G. Dolios, S.-H. Kim, R. Wang, and S. S. Sisodia (2003)
J. Biol. Chem.
278, 7010-7018
|Abstract »|Full Text »|PDF »
Growth Suppression of Pre-T Acute Lymphoblastic Leukemia Cells by Inhibition of Notch Signaling.
A. P. Weng, Y. Nam, M. S. Wolfe, W. S. Pear, J. D. Griffin, S. C. Blacklow, and J. C. Aster (2003)
Mol. Cell. Biol.
23, 655-664
|Abstract »|Full Text »|PDF »
Amyloidogenic processing of the Alzheimer {beta}-amyloid precursor protein depends on lipid rafts.
R. Ehehalt, P. Keller, C. Haass, C. Thiele, and K. Simons (2003)
J. Cell Biol.
160, 113-123
|Abstract »|Full Text »|PDF »
Presenilin-dependent Intramembrane Proteolysis of CD44 Leads to the Liberation of Its Intracellular Domain and the Secretion of an Abeta -like Peptide.
S. Lammich, M. Okochi, M. Takeda, C. Kaether, A. Capell, A.-K. Zimmer, D. Edbauer, J. Walter, H. Steiner, and C. Haass (2002)
J. Biol. Chem.
277, 44754-44759
|Abstract »|Full Text »|PDF »
PEN-2 Is an Integral Component of the gamma -Secretase Complex Required for Coordinated Expression of Presenilin and Nicastrin.
H. Steiner, E. Winkler, D. Edbauer, S. Prokop, G. Basset, A. Yamasaki, M. Kostka, and C. Haass (2002)
J. Biol. Chem.
277, 39062-39065
|Abstract »|Full Text »|PDF »
