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Functional Links Between Aβ Toxicity, Endocytic Trafficking, and Alzheimer’s Disease Risk Factors in Yeast
Open accessAbstract
Aβ (beta-amyloid peptide) is an important contributor to Alzheimer's disease (AD). We modeled Aβ toxicity in yeast by directing the peptide to the secretory pathway. A genome-wide screen for toxicity modifiers identified the yeast homolog of phosphatidylinositol binding clathrin assembly protein (PICALM) and other endocytic factors connected to AD whose relationship to Aβ was previously unknown. The factors identified in yeast modified Aβ toxicity in glutamatergic neurons of Caenorhabditis elegans and in primary rat cortical neurons. In yeast, Aβ impaired the endocytic trafficking of a plasma membrane receptor, which was ameliorated by endocytic pathway factors identified in the yeast screen. Thus, links between Aβ, endocytosis, and human AD risk factors can be ascertained with yeast as a model system.
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“Overexpression of PICALM in the primary rat cortical neurons attenuated the toxicity of soluble A 𝛃 oligomers (598).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [598]
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1 retracted
Liang, Q., Fujita, R., Yamashita, T., Angulo, S. L., Rhinn, H., Rhee, D. B., Doege, C. A., Chau, L., Aubry, L., Vanti, W. B., et al. (2011) · Cell · doi:10.1016/j.cell.2011.07.007 · Cited by 231
RetractedTHE GENETICS OF CAENORHABDITIS ELEGANS
Brenner, S. (1974) · Genetics · doi:10.1093/genetics/77.1.71 · Cited by 15,220
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
A second generation human haplotype map of over 3.1 million SNPs
The International HapMap Consortium (2007) · Nature · doi:10.1038/nature06258 · Cited by 4,438
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326
C. elegans : des neurones et des gènes
Gally, C., & Bessereau, J. (2003) · médecine/sciences · doi:10.1051/medsci/20031967725 · Cited by 3,260
Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease
the European Alzheimer's Disease Initiative Investigators, Lambert, J.-C., Heath, S., Even, G., Campion, D., Sleegers, K., Hiltunen, M., Combarros, O., Zelenika, D., Bullido, M. J., et al. (2009) · Nature Genetics · doi:10.1038/ng.439 · Cited by 2,234
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Items 301–381 of 381
Nazeen, S., Wang, X., Zielinski, D., Lam, I., Hallacli, E., Xu, P., Ethier, E., Strom, R., Zanella, C. A., Nithianandam, V., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.03.583145 · Cited by 5
Self-citationPhytochemicals and Vitagenes for a Healthy Brain
Osakabe, N., Anfuso, C. D., Jacob, U. M., Sidenkova, A. P., Fritsch, T., Abdelhameed, A. S., Rashan, L. J., Wenzel, U., Calabrese, E. J., & Calabrese, V. (2024) · Healthy ageing and longevity · doi:10.1007/978-3-031-68513-2_11 · Cited by 3
From Yeast to Patients: The Audacity and Vision of Susan Lindquist
Khurana, V., Chung, C. Y., & Tardiff, D. F. (2017) · Cell Systems · doi:10.1016/j.cels.2017.02.007 · Cited by 3
Self-citationNew Wine in Old Bottle:Caenorhabditis Elegansin Food Science
Li, Y., Li, P., Zhang, W., Zheng, X., & Gu, Q. (2023) · Food Reviews International · doi:10.1080/87559129.2023.2172429 · Cited by 3
Bao, M., Hua, X., Chen, X., An, T., Mo, H., Sun, Z., Tao, M., Yue, G., & Song, J. (2024) · Advanced Science · doi:10.1002/advs.202401945 · Cited by 3
Santiago-Lopez, A. J., Hovell, C. M., Lee, H., & Kim, Y. (2015) · Biosystems & biorobotics · doi:10.1007/978-3-319-21813-7_13 · Cited by 3
Piotrowski, J. S., & Tardiff, D. F. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9736-7_24 · Cited by 3
Lu, J., Lu, Z., Liu, L., Li, X., Yu, W., & Lu, X. (2021) · Chemistry & Biodiversity · doi:10.1002/cbdv.202100270 · Cited by 4
Endocytic scaffolds at the crossroads of Alzheimer’s disease and neuronal aging
Shergill, J. K., & Tehran, D. A. (2026) · Biological Chemistry · doi:10.1515/hsz-2025-0250 · Cited by 3
Surasiang, T., & Noree, C. (2021) · Biology · doi:10.3390/biology10040294 · Cited by 2
Corbacho‐Cuello, I., García-Prieto, F. F., Hinojosa, A. E., Berrocal, M., & Mata, A. M. (2015) · Protein Expression and Purification · doi:10.1016/j.pep.2015.12.011 · Cited by 2
Derf, A., Mudududdla, R., Bharate, S. B., & Chaudhuri, B. (2018) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2018.11.029 · Cited by 2
Tiny Models to Answer Big Questions: The Worm and the Yeast as Tools in Human Genetics Research
Pardo, P. S., & Walz, K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816573-7.00003-1 · Cited by 2
Ruiz, A., Sánchez, D., Lafuente, A., Ortega, G., Buendía, M., Papasey, J., Jimeno, S. Y., Badia, F. P., Palacio, M. E., Ruiz, C. A., et al. (2022) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2022.38 · Cited by 2
1 Yeast as a Model for Systems Biology Studies on Complex Diseases
Castrillo, J. I., & Oliver, S. G. (2014) · Springer eBooks · doi:10.1007/978-3-642-45218-5_1 · Cited by 2
A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanağası, H. A., Lohmann, E., Samancı, B., Gurvit, H. I., Bılgıç, B., et al. (2021) · Human Genomics · doi:10.1186/s40246-021-00346-z · Cited by 1
Amyloid fibrils are nanoparticles that target lysosomes.
Jakhria, T. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University) · Cited by 2
Genetic Modifiers of Neurological Disease
Kearney, J. A., & Jorge, B. S. (2012) · Wiley eBooks · doi:10.1002/9780470015902.a0023856 · Cited by 3
Role of AMPK in aging and age-related loss of behavioral plasticity in C. elegans
Escoubas, C. C. (2018) · theses.fr (ABES) · doi:10.70675/1c8dd62ez2561z4581zaa55z169311331b91 · Cited by 2
Applications of Nanotechnology in Alzheimer’s Disease
Chountoulesi, M., Naziris, N., Gioran, A., Papagiannopoulos, A., Steele, B. R., Micha‐Screttas, M., Stavrinides, S. G., Hanias, M. P., Chondrogianni, N., Pispas, S., et al. (2023) · Springer eBooks · doi:10.1007/978-3-319-75922-7_16 · Cited by 1
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Prosser, D. C. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202510010 · Cited by 1
Nagarajan, V. D., Libowitz, C. L., Ackley, B. D., & Wolfe, M. S. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107267 · Cited by 2
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Vimal, P., Verma, D., Bhunia, P. K., & Kasturi, P. (2026) · Springer eBooks · doi:10.1007/978-981-92-0038-2_9 · Cited by 2
Cardona, E. A., Webber, C. J., Wu, Z., Bolton, B., Cenik, E. S., & Pierce-Shimomura, J. T. (2026) · Disease Models & Mechanisms · doi:10.1242/dmm.052469 · Cited by 1
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.en.2.132 · Cited by 1
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Vieira, A. V. (2012) · Journal of Physiobiochemical Metabolism · doi:10.4172/2324-8793.1000e106 · Cited by 1
Chen, M., Kretzschmar, D., Verdile, G., & Lardelli, M. T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415894-8.00025-7 · Cited by 2
TDP-43 proteinopathy mechanisms from non-mammalian model systems
Bharathi, V., Girdhar, A., & Patel, B. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820066-7.00002-3 · Cited by 1
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.en.2.116 · Cited by 1
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.pt.2.115 · Cited by 1
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Hayden, E., Chen, S., Chumley, A., Zhong, Q., & Ju, S. (2018) · Journal of Visualized Experiments · doi:10.3791/57978 · Cited by 2
Houang, J., Perrone, G. G., Pedrinazzi, C., Longo, L., Mawad, D., Boughton, P. C., Ruys, A. J., & Lauto, A. (2019) · Photonic Diagnosis, Monitoring, Prevention, and Treatment of Infections and Inflammatory Diseases · doi:10.1117/12.2509284 · Cited by 1
Caenorhabditis elegans as a model organism for protein homeostasis diseases
Good, S. C., & van Oosten‐Hawle, P. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819132-3.00003-8 · Cited by 1
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Marisco, G., Xavier, R., Assunção, R., Amorim, M., Souza, R., & Pungartnik, C. (2021) · Textura · doi:10.22479/texturav14n2p1-13
Watamura, N., Sato, K., Shiihashi, G., Iwasaki, A., Kamano, N., Takahashi, M., Sekiguchi, M., Yamazaki, N., Fujioka, R., Nagata, K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.22.457278 · Cited by 1
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Liu, L. (2014) · Chalmers Publication Library (Chalmers University of Technology) · Cited by 1
Valastyan, J. S. (2013) · DSpace@MIT (Massachusetts Institute of Technology)
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Ehsani, S. (2015) · arXiv (Cornell University) · doi:10.48550/arxiv.1505.03196
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Lord, J., Turton, J. C., Braae, A., Barber, I., Medway, C., Brown, K. S., & Morgan, K. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.05.703
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Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.fr.2.115
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.fr.2.116
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Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.ru.2.115
Ramanan, V. K., & Saykin, A. J. (2013)
Golde, T. E., Lessard, C. B., & Ran, Y. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00005-8
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Bradford, M. K. (2015)
Metabolic study of Alzheimer’s disease using mutant C. elegans
Ahmad, W. (2017) · The University of Queensland · doi:10.14264/uql.2017.500
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Xu, S. (2018) · Figshare
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Bevis, B. J. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy110
Self-citationShakila, G., Meganathan, C., Sundaraganesan, N., & Saleem, H. (2019) · AIP conference proceedings · doi:10.1063/1.5114592
Faculty Opinions recommendation of REST and stress resistance in ageing and Alzheimer's disease.
Moore, S. D. (2014) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718318307.793492518
Arora, M. (2013) · 实验材料和方法 · doi:10.13070/mm.cn.3.175
Johnson, M. (2012) · 实验材料和方法 · doi:10.13070/mm.cn.2.115
Johnson, M. (2012) · 实验材料和方法 · doi:10.13070/mm.cn.2.132
Johnson, M. (2012) · 实验材料和方法 · doi:10.13070/mm.cn.2.116
Lord, J., & Morgan, K. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7309-1_4
Applications of Nanotechnology in Alzheimer’s Disease
Chountoulesi, M., Naziris, N., Gioran, A., Papagiannopoulos, A., Steele, B. R., Micha‐Screttas, M., Stavrinides, S. G., Hanias, M. P., Chondrogianni, N., Pispas, S., et al. (2022) · Springer eBooks · doi:10.1007/978-3-319-75479-6_16-1
Schlein, M. L., Arituluk, Z. C., Stephen, C. A., Caldwell, G. A., Ciesla, L. M., & Caldwell, K. A. (2023) · PubMed Central · doi:10.17912/micropub.biology.000780
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Vig, H., Shukla, P., Mishra, A., Pal, A., & Wal, A. (2024) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/0118715249340567241004043542
Oluwatunase, G. O., Okwute, P. G., Asafa, O. O., Oyeniran, D. A., & Ogenetega, O. B. (2025) · IntechOpen eBooks · doi:10.5772/intechopen.1008845
Cardona, E. A., Webber, C. J., Wu, Z., Bolton, B. M., Cenik, E. S., & Pierce, J. T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.06.652574
Additional file 5 of A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanagasi, H., Lohmann, E., Samancı, B., Gurvit, H. I., Bilgiç, B., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15071686
Additional file 2 of A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanagasi, H., Lohmann, E., Samancı, B., Gurvit, H. I., Bilgiç, B., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15071677
Additional file 1 of A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanagasi, H., Lohmann, E., Samancı, B., Gurvit, H. I., Bilgiç, B., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15071674
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Additional file 3 of A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanagasi, H., Lohmann, E., Samancı, B., Gurvit, H. I., Bilgiç, B., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15071680
Additional file 4 of A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanagasi, H., Lohmann, E., Samancı, B., Gurvit, H. I., Bilgiç, B., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15071683
Additional file 6 of A comprehensive analysis of copy number variation in a Turkish dementia cohort
Dehghani, N., Güven, G., Kun‐Rodrigues, C., Gouveia, C., Foster, K., Hanagasi, H., Lohmann, E., Samancı, B., Gurvit, H. I., Bilgiç, B., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15071689
Choi, H., Lee, S.-M., & Lee, J.-A. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1762891
Stephens, E., Hamza, A., Driessen, M. R. M., O’Neil, N. J., Stirling, P. C., & Hieter, P. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.03.716359
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Mondal, A., & Kural, C. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2026.1844575
Parikh, I. J. (2014) · UKnowledge (University of Kentucky)
Metadata
- Authors
- Treusch, S., Hamamichi, S., Goodman, J. L., Matlack, K. E. S., Chung, C. Y., Baru, V., Shulman, J. M., Parrado, A., Bevis, B. J., Valastyan, J. S., Han, H., Lindhagen-Persson, M., Reiman, E. M., Evans, D. A., Bennett, D. A., Olofsson, A., DeJager, P. L., Tanzi, R. E., Caldwell, K. A., Caldwell, G. A., & Lindquist, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Alabama (US)
- Whitehead Institute for Biomedical Research (US)
- Broad Institute (US)
- Harvard University (US)
- Department of Medical Biochemistry and Biophysics, Umea University, Umea, Sweden.
- Translational Genomics Research Institute (US)
- Rush University Medical Center (US)
- Umeå University (SE)
- Program in Translational NeuroPsychiatric Genomics, Institute for the Neurosciences, Departments of Neurology and Psychiatry, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA.
- Corresponding author
- Lindquist, Susan
- ORCID
- Venue
- Science
- Published
- 2011-12-02
- Volume
- 334
- Issue
- 6060
- Pages
- 1241-1245
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3281757
- OpenAlex
- W2051629075
- Cited by
- 379
- References
- 59
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 13 · 2023: 21 · 2022: 14 · 2021: 20 · 2020: 26 · 2019: 36 · 2018: 27 · 2017: 23 · 2016: 22 · 2015: 32 · 2014: 36 · 2013: 36 · 2012: 52
- FWCI
- 27.49
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute on Aging (R01AG017917, P30-AG 10161, R01‐AG17917, R01 AG15819, K08AG034290, R01AG015819, P30AG010161, P30AG019610)
- National Institute of Neurological Disorders and Stroke (F32NS067782)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta toxicity, Alzheimer's disease, endosomal trafficking, PICALM, yeast model, secretory pathway, plasma membrane receptors, glutamatergic neurons, Caenorhabditis elegans, cortical neurons, Alzheimer's disease risk factors
- MeSH terms
- Alzheimer Disease, Animals, Cell Membrane, Cells, Cultured, Clathrin, Cytoskeleton, Disease Susceptibility, Endocytosis, Genetic Testing, Glutamates, Humans, Neurons, Peptide Fragments, Risk Factors, Saccharomyces cerevisiae, Amyloid beta-Peptides, Caenorhabditis elegans, Protein Transport, Saccharomyces cerevisiae Proteins, Animals, Genetically Modified, Monomeric Clathrin Assembly Proteins, Rats, Protein Multimerization, Secretory Pathway, Genetic Association Studies
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