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Lysosomal Sorting of Amyloid-β by the SORLA Receptor Is Impaired by a Familial Alzheimer’s Disease Mutation

Caglayan, Safak, Takagi-Niidome, Shizuka, Liao, Fan, Carlo, Anne-Sophie, Schmidt, Vanessa, Burgert, Tilman, Kitago, Yu, Füchtbauer, Ernst-Martin, Füchtbauer, Annette, Holtzman, David M., Takagi, Junichi, Willnow, Thomas E.·2014·Science Translational Medicine
DOI 10.1126/scitranslmed.3007747
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Abstract

A familial AD mutation in SORL1 disrupts the ability of the sorting receptor SORLA to mediate intracellular degradation of Aβ peptides.

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Crossref · 10.1126/scitranslmed.3007747

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11 of 11 references verified0 citation errors · 0 not checkable

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  • Transgenic expression of human SORLA reduces Aβ accumulation and pathology in APP/PS1 AD mice.

    “In contrast, transgenic expression of human SORLA reduces Aβ accumulation and pathology in APP/PS1 AD mice (Caglayan, Takagi-Niidome et al. 2014).”

    From SORLA up-regulation suppresses pathological effects in aged tauopathy mouse brain (2026) · cites this paper as Caglayan, Takagi-Niidome et al. 2014

  • SORLA reduces APP and BACE1 interactions while directly binding and facilitating Aβ internalization and lysosomal degradation.

    “In addition, SORLA reduces APP and BACE1 (Spoelgen, von Arnim et al. 2006) interactions while directly binding and facilitating Aβ internalization and lysosomal degradation (Caglayan, Takagi-Niidome et al. 2014, Liu, Zhu et al. 2020).”

    From SORLA up-regulation suppresses pathological effects in aged tauopathy mouse brain (2026) · cites this paper as Caglayan, Takagi-Niidome et al. 2014

  • In addition to trafficking and internalizing Aβ, SORLA may also potentially affect tau accumulation.

    “This suggests that in addition to trafficking and internalizing Aβ (Caglayan, Takagi-Niidome et al. 2014, Liu, Zhu et al. 2020), SORLA may also potentially affect tau accumulation.”

    From SORLA up-regulation suppresses pathological effects in aged tauopathy mouse brain (2026) · cites this paper as Caglayan, Takagi-Niidome et al. 2014

  • SorLA may directly bind nascent Aβ peptides and target them to lysosomes, contributing to the reduction of Aβ secretion.

    “Second, SorLA may directly bind nascent Aβ peptides and target them to lysosomes, which also contributes to the reduction of Aβ secretion [21].”

    From Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease (2021) · cites this paper as [21]

  • To date, only 6 SORL1 missense variants have been studied in vitro and have shown varying degrees of decrease in SorLA protein function.

    “To date, only 6 missense variants have been studied in vitro and have shown varying degrees of decrease in SorLA protein function [21, 28, 29].”

    From Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease (2021) · cites this paper as [21]

Citations

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Research works printed but not linked: 31

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  10. Pottier C., Hannequin D., Coutant S., Rovelet-Lecrux A., Wallon D., Rousseau S., Legallic S., Paquet C., Bombois S., Pariente J., Thomas-Anterion C., Michon A., Croisile B., Etcharry-Bouyx F., Berr C., Dartigues J. F., Amouyel P., Dauchel H., Boutoleau-Bretonnière C., Thauvin C., Frebourg T., Lambert J. C., Campion D., Collaborators P. G., High frequency of potentially pathogenic SORL1 mutations in autosomal dominant early-onset Alzheimer disease. Mol. Psychiatry 17, 875–879 (2012). · DOI · Paper page
  11. Rohe M., Carlo A. S., Breyhan H., Sporbert A., Militz D., Schmidt V., Wozny C., Harmeier A., Erdmann B., Bales K. R., Wolf S., Kempermann G., Paul S. M., Schmitz D., Bayer T. A., Willnow T. E., Andersen O. M., Sortilin-related receptor with A-type repeats (SORLA) affects the amyloid precursor protein-dependent stimulation of ERK signaling and adult neurogenesis. J. Biol. Chem. 283, 14826–14834 (2008). · DOI · Paper page
  12. Kurz A., Perneczky R., Amyloid clearance as a treatment target against Alzheimer’s disease. J. Alzheimers Dis. 24 (Suppl. 2), 61–73 (2011). · DOI
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  14. Zhou B., Zhuang J., Gu D., Wang H., Cebotaru L., Guggino W. B., Cai H., WNK4 enhances the degradation of NCC through a sortilin-mediated lysosomal pathway. J. Am. Soc. Nephrol. 21, 82–92 (2010). · DOI
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  18. Caglayan S., Bauerfeind A., Schmidt V., Carlo A. S., Prabakaran T., Hübner N., Willnow T. E., Identification of Alzheimer disease risk genotype that predicts efficiency of SORL1 expression in the brain. Arch. Neurol. 69, 373–379 (2012). · DOI
  19. Schmidt V., Sporbert A., Rohe M., Reimer T., Rehm A., Andersen O. M., Willnow T. E., SorLA/LR11 regulates processing of amyloid precursor protein via interaction with adaptors GGA and PACS-1. J. Biol. Chem. 282, 32956–32964 (2007). · DOI · Paper page
  20. Fjorback A. W., Seaman M., Gustafsen C., Mehmedbasic A., Gokool S., Wu C., Militz D., Schmidt V., Madsen P., Nyengaard J. R., Willnow T. E., Christensen E. I., Mobley W. B., Nykjær A., Andersen O. M., Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing. J. Neurosci. 32, 1467–1480 (2012). · DOI · Paper page
  21. Small S. A., Retromer sorting: A pathogenic pathway in late-onset Alzheimer disease. Arch. Neurol. 65, 323–328 (2008). · DOI
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  24. Takahashi R. H., Milner T. A., Li F., Nam E. E., Edgar M. A., Yamaguchi H., Beal M. F., Xu H., Greengard P., Gouras G. K., Intraneuronal Alzheimer Aβ42 accumulates in multivesicular bodies and is associated with synaptic pathology. Am. J. Pathol. 161, 1869–1879 (2002). · DOI · Paper page
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  26. Nielsen M. S., Gustafsen C., Madsen P., Nyengaard J. R., Hermey G., Bakke O., Mari M., Schu P., Pohlmann R., Dennes A., Petersen C. M., Sorting by the cytoplasmic domain of the amyloid precursor protein binding receptor SorLA. Mol. Cell. Biol. 27, 6842–6851 (2007). · DOI · Paper page
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  30. Nakata Z., Nagae M., Yasui N., Bujo H., Nogi T., Takagi J., Crystallization and preliminary crystallographic analysis of human LR11 Vps10p domain. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 129–132 (2011). · DOI
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Metadata

Authors
Caglayan, S., Takagi-Niidome, S., Liao, F., Carlo, A.-S., Schmidt, V., Burgert, T., Kitago, Y., Füchtbauer, E.-M., Füchtbauer, A., Holtzman, D. M., Takagi, J., & Willnow, T. E.
Affiliations
  • Max-Delbrueck-Center for Molecular Medicine, 13125 Berlin, Germany.
  • Institute for Protein Research, Osaka University, Osaka 565-0871, Japan.
  • Department of Neurology, Washington University, St. Louis, MO 63110, USA.
  • Department of Molecular Biology, Aarhus University, 8000 Aarhus, Denmark.
Venue
Science Translational Medicine
Publisher
American Association for the Advancement of Science (AAAS)
Published
2014-02-12
Volume
6
Issue
223
ISSN
  • 1946-6234
  • 1946-6242
DOI
10.1126/scitranslmed.3007747
Cited by
166
References
11
Language
en

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