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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Line V. Kristensen
  • Felix S. Oppermann
  • Matthias J. Rauen
  • Karina Fog
  • Thorsten Schmidt
  • Jana Schmidt
  • Tina Harmuth
  • Hartmann-Petersen, Rasmus
  • Kenneth Thirstrup

Deubiquitinating enzymes (DUBs) play important roles in a variety of cellular processes, including regulation of protein homeostasis. The DUB ataxin-3 is an enzyme implicated in protein quality control mechanisms. 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. Increasing the understanding of ataxin-3 protein interaction partners could help to elucidate disease mechanisms. Hence, we analyzed the repertoire of proteins interacting with normal and polyQ expanded ataxin-3 by mass spectrometry. This showed that both normal and polyQ expanded ataxin-3 interacted with components of the protein quality control system and mitochondria. Five proteins showed increased interaction with polyQ expanded ataxin-3 relative to normal and three of these were mitochondrial proteins. The analyses underline the role of ataxin-3 in ubiquitin biology and point towards a role in mitochondrial biology.

OriginalsprogEngelsk
TidsskriftNeurochemistry International
Vol/bind112
Sider (fra-til)5-17
Antal sider13
ISSN0197-0186
DOI
StatusUdgivet - jan. 2018

ID: 186088130