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Restricted Location of PSEN2/γ-Secretase Determines Substrate Specificity and Generates an Intracellular Aβ Pool

Sannerud, Ragna, Esselens, Cary, Ejsmont, Paulina, Mattera, Rafael, Rochin, Leila, Tharkeshwar, Arun Kumar, De Baets, Greet, De Wever, Veerle, Habets, Roger, Baert, Veerle, Vermeire, Wendy, Michiels, Christine, Groot, Arjan J., Wouters, Rosanne, Dillen, Katleen, Vints, Katlijn, Baatsen, Pieter, Munck, Sebastian, Derua, Rita, Waelkens, Etienne, Basi, Guriqbal S., Mercken, Mark, Vooijs, Marc, Bollen, Mathieu, Schymkowitz, Joost, Rousseau, Frederic, Bonifacino, Juan S., Van Niel, Guillaume, De Strooper, Bart, Annaert, Wim·2016·Cell

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  1. Acx, 2014, Signature amyloid β profiles are produced by different γ-secretase complexes, J. Biol. Chem., 289, 4346, 10.1074/jbc.M113.530907 · DOI
  2. Bayer, 2011, Intraneuronal Aβ as a trigger for neuron loss: can this be translated into human pathology?, Biochem. Soc. Trans., 39, 857, 10.1042/BST0390857 · DOI
  3. Bentahir, 2006, Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms, J. Neurochem., 96, 732, 10.1111/j.1471-4159.2005.03578.x · DOI
  4. Bonifacino, 2014, Adaptor proteins involved in polarized sorting, J. Cell Biol., 204, 7, 10.1083/jcb.201310021 · DOI
  5. Braulke, 2009, Sorting of lysosomal proteins, Biochim. Biophys. Acta, 1793, 605, 10.1016/j.bbamcr.2008.10.016 · DOI · Paper page
  6. Canevelli, 2014, Familial Alzheimer’s disease sustained by presenilin 2 mutations: systematic review of literature and genotype-phenotype correlation, Neurosci. Biobehav. Rev., 42, 170, 10.1016/j.neubiorev.2014.02.010 · DOI · Paper page
  7. Cataldo, 2000, Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer’s disease and Down syndrome: differential effects of APOE genotype and presenilin mutations, Am. J. Pathol., 157, 277, 10.1016/S0002-9440(10)64538-5 · DOI · Paper page
  8. Chávez-Gutiérrez, 2012, The mechanism of γ-secretase dysfunction in familial Alzheimer disease, EMBO J., 31, 2261, 10.1038/emboj.2012.79 · DOI · Paper page
  9. Cruts, 2012, Locus-specific mutation databases for neurodegenerative brain diseases, Hum. Mutat., 33, 1340, 10.1002/humu.22117 · DOI
  10. De Strooper, 2010, Novel research horizons for presenilins and γ-secretases in cell biology and disease, Annu. Rev. Cell Dev. Biol., 26, 235, 10.1146/annurev-cellbio-100109-104117 · DOI
  11. Edbauer, 2003, Reconstitution of gamma-secretase activity, Nat. Cell Biol., 5, 486, 10.1038/ncb960 · DOI
  12. Esbjörner, 2014, Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation, Chem. Biol., 21, 732, 10.1016/j.chembiol.2014.03.014 · DOI
  13. Farías, 2012, Signal-mediated, AP-1/clathrin-dependent sorting of transmembrane receptors to the somatodendritic domain of hippocampal neurons, Neuron, 75, 810, 10.1016/j.neuron.2012.07.007 · DOI · Paper page
  14. Freeman, 2014, The rhomboid-like superfamily: molecular mechanisms and biological roles, Annu. Rev. Cell Dev. Biol., 30, 235, 10.1146/annurev-cellbio-100913-012944 · DOI · Paper page
  15. Ginsberg, 2010, Microarray analysis of hippocampal CA1 neurons implicates early endosomal dysfunction during Alzheimer’s disease progression, Biol. Psychiatry, 68, 885, 10.1016/j.biopsych.2010.05.030 · DOI · Paper page
  16. Golde, 2009, Signal peptide peptidases: a family of intramembrane-cleaving proteases that cleave type 2 transmembrane proteins, Semin. Cell Dev. Biol., 20, 225, 10.1016/j.semcdb.2009.02.003 · DOI
  17. Jia, 2014, Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1, eLife, 3, e02362, 10.7554/eLife.02362 · DOI
  18. Jurisch-Yaksi, 2013, A fast growing spectrum of biological functions of γ-secretase in development and disease, Biochim. Biophys. Acta, 1828, 2815, 10.1016/j.bbamem.2013.04.016 · DOI
  19. Karch, 2015, Alzheimer’s disease risk genes and mechanisms of disease pathogenesis, Biol. Psychiatry, 77, 43, 10.1016/j.biopsych.2014.05.006 · DOI · Paper page
  20. Kashatus, 2011, RALA and RALBP1 regulate mitochondrial fission at mitosis, Nat. Cell Biol., 13, 1108, 10.1038/ncb2310 · DOI · Paper page
  21. Kelly, 2008, A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex, Nature, 456, 976, 10.1038/nature07422 · DOI
  22. Kopan, 2004, Gamma-secretase: proteasome of the membrane?, Nat. Rev. Mol. Cell Biol., 5, 499, 10.1038/nrm1406 · DOI
  23. Krawitz, 2005, Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3, J. Biol. Chem., 280, 39515, 10.1074/jbc.M501645200 · DOI
  24. Krieger, 2002, Increasing the precision of comparative models with YASARA NOVA--a self-parameterizing force field, Proteins, 47, 393, 10.1002/prot.10104 · DOI
  25. Maes, 2014, Tumor vessel normalization by chloroquine independent of autophagy, Cancer Cell, 26, 190, 10.1016/j.ccr.2014.06.025 · DOI
  26. Mattera, 2011, Conservation and diversification of dileucine signal recognition by adaptor protein (AP) complex variants, J. Biol. Chem., 286, 2022, 10.1074/jbc.M110.197178 · DOI
  27. Nikonova, 2013, Aurora A kinase (AURKA) in normal and pathological cell division, Cell. Mol. Life Sci., 70, 661, 10.1007/s00018-012-1073-7 · DOI
  28. Peden, 2004, Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins, J. Cell Biol., 164, 1065, 10.1083/jcb.200311064 · DOI
  29. Pensalfini, 2014, Intracellular amyloid and the neuronal origin of Alzheimer neuritic plaques, Neurobiol. Dis., 71, 53, 10.1016/j.nbd.2014.07.011 · DOI · Paper page
  30. Perez, 1999, Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42, J. Biol. Chem., 274, 18851, 10.1074/jbc.274.27.18851 · DOI
  31. Peric, 2015, Early etiology of Alzheimer’s disease: tipping the balance toward autophagy or endosomal dysfunction?, Acta Neuropathol., 129, 363, 10.1007/s00401-014-1379-7 · DOI
  32. Plotnikova, 2010, Rapid calcium-dependent activation of Aurora-A kinase, Nat. Commun., 1, 64, 10.1038/ncomms1061 · DOI
  33. Raposo, 2007, Melanosomes—dark organelles enlighten endosomal membrane transport, Nat. Rev. Mol. Cell Biol., 8, 786, 10.1038/nrm2258 · DOI
  34. Saftig, 2009, Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function, Nat. Rev. Mol. Cell Biol., 10, 623, 10.1038/nrm2745 · DOI · Paper page
  35. Sannerud, 2009, Trafficking, a key player in regulated intramembrane proteolysis, Semin. Cell Dev. Biol., 20, 183, 10.1016/j.semcdb.2008.11.004 · DOI
  36. Serneels, 2005, Differential contribution of the three Aph1 genes to gamma-secretase activity in vivo, Proc. Natl. Acad. Sci. USA, 102, 1719, 10.1073/pnas.0408901102 · DOI
  37. Serneels, 2009, gamma-Secretase heterogeneity in the Aph1 subunit: relevance for Alzheimer’s disease, Science, 324, 639, 10.1126/science.1171176 · DOI
  38. Tagami, 2008, Regulation of Notch signaling by dynamic changes in the precision of S3 cleavage of Notch-1, Mol. Cell. Biol., 28, 165, 10.1128/MCB.00863-07 · DOI
  39. Takahashi, 2002, Alzheimer beta-amyloid peptides: normal and abnormal localization, Histol. Histopathol., 17, 239
  40. Takasugi, 2003, The role of presenilin cofactors in the gamma-secretase complex, Nature, 422, 438, 10.1038/nature01506 · DOI
  41. Takitoh, 2012, Activation of Aurora-A is essential for neuronal migration via modulation of microtubule organization, J. Neurosci., 32, 11050, 10.1523/JNEUROSCI.5664-11.2012 · DOI
  42. Traub, 2013, Cargo recognition in clathrin-mediated endocytosis, Cold Spring Harb. Perspect. Biol., 5, a016790, 10.1101/cshperspect.a016790 · DOI
  43. Voss, 2013, Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases, Biochim. Biophys. Acta, 1828, 2828, 10.1016/j.bbamem.2013.03.033 · DOI
  44. Walter, 1996, The Alzheimer’s disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum, Mol. Med., 2, 673, 10.1007/BF03401652 · DOI
  45. Wang, 2006, Regulation of tyrosinase trafficking and processing by presenilins: partial loss of function by familial Alzheimer’s disease mutation, Proc. Natl. Acad. Sci. USA, 103, 353, 10.1073/pnas.0509822102 · DOI
  46. Watt, 2013, PMEL: a pigment cell-specific model for functional amyloid formation, Pigment Cell Melanoma Res., 26, 300, 10.1111/pcmr.12067 · DOI
  47. Wolfe, 2009, Intramembrane-cleaving proteases, J. Biol. Chem., 284, 13969, 10.1074/jbc.R800039200 · DOI

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Metadata

Authors
Sannerud, R., Esselens, C., Ejsmont, P., Mattera, R., Rochin, L., Tharkeshwar, A. K., De Baets, G., De Wever, V., Habets, R., Baert, V., Vermeire, W., Michiels, C., Groot, A. J., Wouters, R., Dillen, K., Vints, K., Baatsen, P., Munck, S., Derua, R., Waelkens, E., Basi, G. S., Mercken, M., Vooijs, M., Bollen, M., Schymkowitz, J., Rousseau, F., Bonifacino, J. S., Van Niel, G., De Strooper, B., & Annaert, W.
Venue
Cell
Publisher
Elsevier BV
Published
2016-06
Volume
166
Issue
1
Pages
193-208
ISSN
0092-8674
Cited by
299
References
6
Language
en

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