Title : Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function.

Pub. Date : 2018 Jan

PMID : 29111377






8 Functional Relationships(s)
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1 Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. polyglutamine ataxin 3 Homo sapiens
2 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine ataxin 3 Homo sapiens
3 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine ataxin 3 Homo sapiens
4 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine ataxin 3 Homo sapiens
5 In the neurodegenerative disease spinocerebellar ataxia type 3 (SCA3), ataxin-3 contains an expanded polyglutamine (polyQ) stretch that leads to aggregation of the protein and neuronal dysfunction. polyglutamine ataxin 3 Homo sapiens
6 Hence, we analyzed the repertoire of proteins interacting with normal and polyQ expanded ataxin-3 by mass spectrometry. polyglutamine ataxin 3 Homo sapiens
7 This showed that both normal and polyQ expanded ataxin-3 interacted with components of the protein quality control system and mitochondria. polyglutamine ataxin 3 Homo sapiens
8 Five proteins showed increased interaction with polyQ expanded ataxin-3 relative to normal and three of these were mitochondrial proteins. polyglutamine ataxin 3 Homo sapiens