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

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Standard

Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. / Kristensen, Line V.; Oppermann, Felix S.; Rauen, Matthias J.; Fog, Karina; Schmidt, Thorsten; Schmidt, Jana; Harmuth, Tina; Hartmann-Petersen, Rasmus; Thirstrup, Kenneth.

I: Neurochemistry International, Bind 112, 01.2018, s. 5-17.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Kristensen, LV, Oppermann, FS, Rauen, MJ, Fog, K, Schmidt, T, Schmidt, J, Harmuth, T, Hartmann-Petersen, R & Thirstrup, K 2018, 'Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function', Neurochemistry International, bind 112, s. 5-17. https://doi.org/10.1016/j.neuint.2017.10.013

APA

Kristensen, L. V., Oppermann, F. S., Rauen, M. J., Fog, K., Schmidt, T., Schmidt, J., Harmuth, T., Hartmann-Petersen, R., & Thirstrup, K. (2018). Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. Neurochemistry International, 112, 5-17. https://doi.org/10.1016/j.neuint.2017.10.013

Vancouver

Kristensen LV, Oppermann FS, Rauen MJ, Fog K, Schmidt T, Schmidt J o.a. Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. Neurochemistry International. 2018 jan.;112:5-17. https://doi.org/10.1016/j.neuint.2017.10.013

Author

Kristensen, Line V. ; Oppermann, Felix S. ; Rauen, Matthias J. ; Fog, Karina ; Schmidt, Thorsten ; Schmidt, Jana ; Harmuth, Tina ; Hartmann-Petersen, Rasmus ; Thirstrup, Kenneth. / Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function. I: Neurochemistry International. 2018 ; Bind 112. s. 5-17.

Bibtex

@article{b9bb4aa27fc44037a53863e0a8baa89c,

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

abstract = "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.",

keywords = "Journal Article",

author = "Kristensen, {Line V.} and Oppermann, {Felix S.} and Rauen, {Matthias J.} and Karina Fog and Thorsten Schmidt and Jana Schmidt and Tina Harmuth and Rasmus Hartmann-Petersen and Kenneth Thirstrup",

year = "2018",

month = jan,

doi = "10.1016/j.neuint.2017.10.013",

language = "English",

volume = "112",

pages = "5--17",

journal = "Neurochemistry International",

issn = "0197-0186",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function

AU - Kristensen, Line V.

AU - Oppermann, Felix S.

AU - Rauen, Matthias J.

AU - Fog, Karina

AU - Schmidt, Thorsten

AU - Schmidt, Jana

AU - Harmuth, Tina

AU - Hartmann-Petersen, Rasmus

AU - Thirstrup, Kenneth

PY - 2018/1

Y1 - 2018/1

N2 - 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.

AB - 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.

KW - Journal Article

U2 - 10.1016/j.neuint.2017.10.013

DO - 10.1016/j.neuint.2017.10.013

M3 - Journal article

C2 - 29111377

VL - 112

SP - 5

EP - 17

JO - Neurochemistry International

JF - Neurochemistry International

SN - 0197-0186

ER -

ID: 186088130

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