Ontology highlight
ABSTRACT:
SUBMITTER: Yu A
PROVIDER: S-EPMC3992642 | biostudies-literature | 2014 Apr
REPOSITORIES: biostudies-literature
Yu Anan A Shibata Yoko Y Shah Bijal B Calamini Barbara B Lo Donald C DC Morimoto Richard I RI
Proceedings of the National Academy of Sciences of the United States of America 20140401 15
Protein conformational diseases exhibit complex pathologies linked to numerous molecular defects. Aggregation of a disease-associated protein causes the misfolding and aggregation of other proteins, but how this interferes with diverse cellular pathways is unclear. Here, we show that aggregation of neurodegenerative disease-related proteins (polyglutamine, huntingtin, ataxin-1, and superoxide dismutase-1) inhibits clathrin-mediated endocytosis (CME) in mammalian cells by aggregate-driven sequest ...[more]