Presenilins and the intramembrane proteolysis of proteins: facts and fiction (original) (raw)

• Wurtman, R. J. Alzheimer's disease. Sci. Am. 252, 62–66 (1985).
  Article CAS PubMed Google Scholar
• Sherrington, R. et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature 375, 754–760 (1995).
  Article CAS PubMed Google Scholar
• Levy-Lahad, E. et al. Candidate gene for the chromosome 1 familial Alzheimer's disease locus. Science 269, 973–977 (1995).
  Article CAS PubMed Google Scholar
• Rogaev, E. I. et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome 1 related to the Alzheimer's disease type 3 gene. Nature 376, 775–778 (1995).
  Article CAS PubMed Google Scholar
• Doan, A. et al. Protein topology of presenilin 1. Neuron 17, 1023–1030 (1996).
  Article CAS PubMed Google Scholar
• Li, X. & 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).
  Article CAS PubMed PubMed Central Google Scholar
• Thinakaran, G. et al. Evidence that levels of presenilins (PS1 and PS2) are coordinately regulated by competition for limiting cellular factors. J. Biol. Chem. 272, 28415–28422 (1997).
  Article CAS PubMed Google Scholar
• Thinakaran et al. Endoproteolysis of presenilin 1 and accumulation of processed derivatives in vivo. Neuron 17, 181–190 (1996).
  Article CAS PubMed Google Scholar
• Capell, A. et al. The proteolytic fragments of the Alzheimer's disease-associated presenilin-1 form heterodimers and occur as a 100–150-kDa molecular mass complex. J. Biol. Chem. 273, 3205–3211 (1998).
  Article CAS PubMed Google Scholar
• Kim, T. W. et al. Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J. Biol. Chem. 272, 11006–11010 (1997).
  Article CAS PubMed Google Scholar
• Yu, G. et al. The presenilin 1 protein is a component of a high molecular weight intracellular complex that contains β-catenin. J. Biol. Chem. 273, 16470–16475 (1998).
  Article CAS PubMed Google Scholar
• Yu, G. et al. Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes. J. Biol. Chem. 275, 27348–27353 (2000).
  CAS PubMed Google Scholar
• Steiner, H. et al. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem. 273, 32322–32331 (1998).
  Article CAS PubMed Google Scholar
• Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing. Nature 407, 48–54 (2000).
  Article CAS PubMed Google Scholar
• Zhou, J. et al. Presenilin 1 interaction in the brain with a novel member of the Armadillo family. NeuroReport 8, 1489–1494 (1997).
  Article CAS PubMed Google Scholar
• Saura, C. A. et al. The nonconserved hydrophilic loop domain of presenilin (PS) is not required for PS endoproteolysis or enhanced Aβ42 production mediated by familial early onset Alzheimer's disease-linked PS variants. J. Biol. Chem. 275, 17136–17142 (2000).
  Article CAS PubMed Google Scholar
• Soriano, S. et al. Presenilin 1 negatively regulates β-catenin/T cell factor/lymphoid enhancer factor-1 signaling independently of β-amyloid precursor protein and Notch processing. J. Cell Biol. 152, 785–794 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Selkoe, D. J. Notch and presenilins in vertebrates and invertebrates: implications for neuronal development and degeneration. Curr. Opin. Neurobiol. 10, 50–57 (2000).
  Article CAS PubMed Google Scholar
• Wong, P. C. et al. Presenilin 1 is required for Notch1 and DII1 expression in the paraxial mesoderm. Nature 387, 288–292 (1997).
  Article CAS PubMed Google Scholar
• Shen, J. et al. Skeletal and CNS defects in Presenilin-1-deficient mice. Cell 89, 629–639 (1997).
  Article CAS PubMed Google Scholar
• Xia, X. et al. Loss of presenilin 1 is associated with enhanced β-catenin signaling and skin tumorigenesis. Proc. Natl Acad. Sci. (in the press).
• De Strooper, B. & Annaert, W. Where Notch and Wnt signaling meet. The presenilin hub. J. Cell Biol. 152, F17–F20 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Vito, P., Lacana, E. & D'Adamio, L. Interfering with apoptosis: Ca-binding protein Alg-2 and Alzheimer's disease gene Alg-3. Science 271, 521–525 (1996).
  Article CAS PubMed Google Scholar
• Katayama, T. et al. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nature Cell Biol. 1, 479–485 (1999).
  Article CAS PubMed Google Scholar
• Niwa, M., Sidrauski, C., Kaufman, R. J. & Walter, P. A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response. Cell 99, 691–702 (1999).
  Article CAS PubMed Google Scholar
• Leissring, M. A. et al. Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice. J. Cell Biol. 149, 793–798 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Yoo, A. S. et al. Presenilin-mediated modulation of capacitative calcium entry. Neuron 27, 561–572 (2000).
  Article CAS PubMed Google Scholar
• Yu, H. et al. APP processing and synaptic plasticity in the adult cerebral cortex of presenilin-1 conditional knock out mice. Neuron (in the press).
• Sato, N. et al. Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression. Nature Cell Biol. 2, 863–870 (2000).
  Article CAS PubMed Google Scholar
• Gu, Y. et al. Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase-like cleavage of Notch. J. Biol. Chem. 10.1074/jbc.C100357200 (2001).
• Pinnix, I. et al. A novel γ-secretase assay based on detection of the putative C-terminal fragment-γ of amyloid β protein precursor. J. Biol. Chem. 276, 481–487 (2001).
  Article CAS PubMed Google Scholar
• Sastre, M. et al. Presenilin-dependent γ-secretase processing of β-Amyloid precursor protein at a site corresponding to the S3 cleavage of Notch. EMBO Rep. (in the press).
• Lichtenthaler, S. F. et al. Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. Proc. Natl Acad. Sci. USA 96, 3053–3058 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Scheuner, D. et al. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2, 864–870 (1996).
  Article CAS PubMed Google Scholar
• De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387–390 (1998).
  Article CAS PubMed Google Scholar
• Naruse, S. et al. Effects of PS1 deficiency on membrane protein trafficking in neurons. Neuron 21, 1213–1221 (1998).
  Article CAS PubMed Google Scholar
• Zhang, Z. et al. Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1. Nature Cell Biol. 2, 463–465 (2000).
  Article CAS PubMed Google Scholar
• Herreman, A. et al. Total inactivation of γ-secretase activity in presenilin-deficient embryonic stem cells. Nature Cell Biol. 2, 461–462 (2000).
  Article CAS PubMed Google Scholar
• Armogida, M. et al. Endogeneous β-amyloid production in presenilin-deficient embryonic mice fibroblasts. Nature Cell Biol. (in the press).
• Annaert, W. G. et al. Presenilin 1 controls γ-secretase processing of amyloid precursor protein in pre-golgi compartments of hippocampal neurons. J. Cell Biol. 147, 277–294 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Li, Y. M. et al. Presenilin 1 is linked with γ-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA 97, 6138–6143 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Seiffert, D. et al. Presenilin-1 and -2 are molecular targets for γ-secretase inhibitors. J. Biol. Chem. 275, 34086–34091 (2000).
  Article CAS PubMed Google Scholar
• Palacino, J. J. et al. Regulation of amyloid precursor protein processing by presenilin 1 (PS1) and PS2 in PS1 knockout cells. J. Biol. Chem. 275, 215–222 (2000).
  Article CAS PubMed Google Scholar
• Wolfe, M. S. et al. Peptidomimetic probes and molecular modeling suggest that Alzheimer's γ-secretase is an intramembrane-cleaving aspartyl protease. Biochemistry 38, 4720–4727 (1999).
  Article CAS PubMed Google Scholar
• Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenelin endoproteolysis and γ-secretase activity. Nature 398, 513–517 (1999).
  Article CAS PubMed Google Scholar
• Steiner, H. et al. Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases. Nature Cell Biol. 2, 848–851 (2000).
  Article CAS PubMed Google Scholar
• Esler, W. P. et al. Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1. Nature Cell Biol. 2, 428–434 (2000).
  Article CAS PubMed Google Scholar
• Li, Y. M. et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689–694 (2000).
  Article CAS PubMed Google Scholar
• De Strooper, B. et al. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain. Nature 398, 518–522 (1999).
  Article CAS PubMed Google Scholar
• Struhl, G. & Greenwald, I. Presenilin is required for activity and nuclear access of Notch in Drosophila. Nature 398, 522–525 (1999).
  Article CAS PubMed Google Scholar
• Annaert, W. & De Strooper, B. Presenilins: molecular switches between proteolysis and signal transduction. Trends Neurosci. 22, 439–443 (1999).
  Article CAS PubMed Google Scholar
• Cupers, P., Orlans, I., Craessaerts, K., Annaert, W. & De Strooper, B. The amyloid precursor protein (APP)-cytoplasmic fragment generated by γ-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurones in culture. J. Neurochem. 78, 1168–1178
• Cao, X. & Sudhof, T. C. A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115–120 (2001).
  Article CAS PubMed Google Scholar
• Capell, A. et al. Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch. Nature Cell Biol. 2, 205–211 (2000).
  Article CAS PubMed Google Scholar
• Morihara, T. et al. Absence of endoproteolysis but no effects on amyloid β production by alternative splicing forms of presenilin-1, which lack exon 8 and replace D257A. Brain Res. Mol. Brain Res. 85, 85–90 (2000).
  Article CAS PubMed Google Scholar
• Petit, A. et al. New protease inhibitors prevent γ-secretase-mediated production of Aβ40/42 without affecting Notch cleavage. Nature Cell Biol. 3, 507–511 (2001).
  Article CAS PubMed Google Scholar
• Citron, M. et al. Inhibition of amyloid β-protein production in neural cells by the serine protease inhibitor AEBSF. Neuron 17, 171–179 (1996).
  Article CAS PubMed Google Scholar
• Vassar, R. et al. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735–741 (1999).
  Article CAS PubMed Google Scholar
• Huppert, S. S. et al. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1. Nature 405, 966–970 (2000).
  Article CAS PubMed Google Scholar
• Murphy, M. P. et al. Presenilin 1 regulates pharmacologically distinct γ-secretase activities. Implications for the role of presenilin in γ-secretase cleavage. J. Biol. Chem. 275, 26277–26284 (2000).
  Article CAS PubMed Google Scholar
• Brown, M. S. & Goldstein, J. L. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89, 331–340 (1997).
  Article CAS PubMed Google Scholar
• Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391–398 (2000).
  Article CAS PubMed Google Scholar
• Sakai, J. et al. Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol. Cell 2, 505–514 (1998).
  Article CAS PubMed Google Scholar
• Rawson, R. B. et al. Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs. Mol. Cell 1, 47–57 (1997).
  Article CAS PubMed Google Scholar
• Ye, J. et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6, 1355–1364 (2000).
  Article CAS PubMed Google Scholar
• Cupers, P. et al. The discrepancy between presenilin subcellular localization and γ-secretase processing of amyloid precursor protein. J Cell Biol 154, 731–740 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Ray, W. J. et al. Cell surface presenilin-1 participates in the γ-secretase-like proteolysis of notch. J. Biol. Chem. 274, 36801–36807 (1999).
  Article CAS PubMed Google Scholar
• Thinakaran, G. et al. Stable association of presenilin derivatives and absence of presenilin interactions with APP. Neurobiol. Dis. 4, 438–453 (1998).
  Article CAS PubMed Google Scholar
• Lammich, S. et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl Acad. Sci. USA 96, 3922–3927 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Buxbaum, J. D. et al. Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273, 27765–27767 (1998).
  Article CAS PubMed Google Scholar
• Struhl, G. & Adachi, A. Requirements for presenilin-dependent cleavage of notch and other transmembrane proteins. Mol. Cell 6, 625–636 (2000).
  Article CAS PubMed Google Scholar
• Logeat, F. et al. The Notch1 receptor is cleaved constitutively by a furin-like convertase. Proc. Natl Acad. Sci. USA 95, 8108–8112 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Brou, C. et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol. Cell 5, 207–216 (2000).
  Article CAS PubMed Google Scholar
• Mumm, J. S. et al. A ligand-induced extracellular cleavage regulates γ-secretase-like proteolytic activation of Notch1. Mol. Cell 5, 197–206 (2000).
  Article CAS PubMed Google Scholar
• Yang, T., Goldstein, J. L. & Brown, M. S. Overexpression of membrane domain of SCAP prevents sterols from inhibiting SCAP.SREBP exit from endoplasmic reticulum. J. Biol. Chem. 275, 29881–29886 (2000).
  Article CAS PubMed Google Scholar
• Nohturfft, A., Yabe, D., Goldstein, J. L., Brown, M. S. & Espenshade, P. J. Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes. Cell 102, 315–323 (2000).
  Article CAS PubMed Google Scholar
• Duncan, E. A., Dave, U. P., Sakai, J., Goldstein, J. L. & Brown, M. S. Second-site cleavage in sterol regulatory element-binding protein occurs at transmembrane junction as determined by cysteine panning. J. Biol. Chem. 273, 17801–17809 (1998).
  Article CAS PubMed Google Scholar
• Xia, W. et al. Presenilin complexes with the C-terminal fragments of amyloid precursor protein at the sites of amyloid β-protein generation. Proc. Natl Acad. Sci. USA 97, 9299–9304 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Weidemann, A. et al. Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and β-amyloid precursor protein. Nature Med. 3, 328–332 (1997).
  Article CAS PubMed Google Scholar
• Fassbender, K. et al. Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo. Proc. Natl Acad. Sci. USA 98, 5856–5861 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Maltese, W. A. et al. Retention of the Alzheimer's amyloid precursor protein fragment C99 in the endoplasmic reticulum prevents formation of amyloid β-peptide. J. Biol. Chem. 276, 20267–20279 (2001).
  Article CAS PubMed Google Scholar
• Iwata, H., Tomita, T., Maruyama, K. & Iwatsubo, T. Subcellular compartment and molecular subdomain of β-amyloid precursor protein relevant to the Aβ42-promoting effects of Alzheimer mutant presenilin 2. J. Biol. Chem. 276, 21678–21685 (2001).
  Article CAS PubMed Google Scholar