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Functional Links Between Aβ Toxicity, Endocytic Trafficking, and Alzheimer’s Disease Risk Factors in Yeast
Functional Links Between Aβ Toxicity, Endocytic Trafficking, and Alzheimer’s Disease Risk Factors in Yeast
- Source :
- Science. 334:1241-1245
- Publication Year :
- 2011
- Publisher :
- American Association for the Advancement of Science (AAAS), 2011.
-
Abstract
- 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.
- Subjects :
- Saccharomyces cerevisiae Proteins
Endocytic cycle
Saccharomyces cerevisiae
Biology
Endocytosis
Clathrin
PICALM
Animals, Genetically Modified
Glutamates
Alzheimer Disease
Risk Factors
Animals
Humans
Genetic Testing
Caenorhabditis elegans
Cells, Cultured
Cytoskeleton
Genetic Association Studies
Secretory pathway
Neurons
Amyloid beta-Peptides
Secretory Pathway
Multidisciplinary
Cell Membrane
Phosphatidylinositol binding
P3 peptide
Peptide Fragments
Yeast
Rats
Cell biology
Protein Transport
Biochemistry
Monomeric Clathrin Assembly Proteins
biology.protein
Disease Susceptibility
Protein Multimerization
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 334
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....594848704371a403f8184ef52b262667
- Full Text :
- https://doi.org/10.1126/science.1213210