Quantification of Ataxin-3 and Ataxin-7 aggregates formed in vivo in Drosophila reveals a threshold of aggregated polyglutamine proteins associated with cellular toxicity

• Published in: Biochemical and biophysical research communications Vol. 464; no. 4; pp. 1060 - 1065
• Main Authors: Vinatier, Gérald, Corsi, Jean-Marc, Mignotte, Bernard, Gaumer, Sébastien
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 04.09.2015; Elsevier
• Subjects: Aging - genetics; Aging - metabolism; Aging - pathology; Animals; Animals, Genetically Modified; Ataxin-3 - chemistry; Ataxin-3 - genetics; Ataxin-3 - metabolism; Ataxin-7 - chemistry; Ataxin-7 - genetics; Ataxin-7 - metabolism; cell death; cytotoxicity; Disease Models, Animal; Drosophila; Drosophila melanogaster; Drosophila melanogaster - genetics; Drosophila melanogaster - metabolism; Female; Heredodegenerative Disorders, Nervous System - genetics; Heredodegenerative Disorders, Nervous System - metabolism; Heredodegenerative Disorders, Nervous System - pathology; Humans; Life Sciences; Male; Models, Neurological; Mutant Proteins - chemistry; Mutant Proteins - genetics; Mutant Proteins - metabolism; Peptides - chemistry; Peptides - genetics; Peptides - metabolism; Polyglutamine disease; Protein Aggregates; Protein Aggregation, Pathological - genetics; Protein Aggregation, Pathological - metabolism; proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Repressor Proteins - chemistry; Repressor Proteins - genetics; Repressor Proteins - metabolism; SCA3; SCA7; Solubility; Polyglutamine disease; SCA7; SCA3; Drosophila melanogaster; Protein aggregates

Polyglutamine diseases are nine dominantly inherited neurodegenerative pathologies caused by the expansion of a polyglutamine domain in a protein responsible for the disease. This expansion leads to protein aggregation, inclusion formation and toxicity. Despite numerous studies focusing on the subje...