SUMOylation by SUMO2 is implicated in the degradation of misfolded ataxin-7 via RNF4 in SCA7 models
Perturbation of protein homeostasis and aggregation of misfolded proteins is a major cause of many human diseases. A hallmark of the neurodegenerative disease spinocerebellar ataxia type 7 (SCA7) is the intranuclear accumulation of mutant, misfolded ataxin-7 (polyQ-ATXN7). Here, we show that endogen...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
11 January 2019
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| In: |
Disease models & mechanisms
Year: 2019, Jahrgang: 12, Heft: 1, Pages: 1-16 |
| ISSN: | 1754-8411 |
| DOI: | 10.1242/dmm.036145 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.1242/dmm.036145 Verlag, Volltext: http://dmm.biologists.org/content/12/1/dmm036145 
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| Verfasserangaben: | Martina Marinello, Andreas Werner, Mariagiovanna Giannone, Khadija Tahiri, Sandro Alves, Christelle Tesson, Wilfred den Dunnen, Jacob-S. Seeler, Alexis Brice and Annie Sittler |
| Zusammenfassung: | Perturbation of protein homeostasis and aggregation of misfolded proteins is a major cause of many human diseases. A hallmark of the neurodegenerative disease spinocerebellar ataxia type 7 (SCA7) is the intranuclear accumulation of mutant, misfolded ataxin-7 (polyQ-ATXN7). Here, we show that endogenous ATXN7 is modified by SUMO proteins, thus also suggesting a physiological role for this modification under conditions of proteotoxic stress caused by the accumulation of polyQ-ATXN7. Co-immunoprecipitation experiments, immunofluorescence microscopy and proximity ligation assays confirmed the colocalization and interaction of polyQ-ATXN7 with SUMO2 in cells. ... |
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| Beschreibung: | Gesehen am 16.05.2019 |
| Beschreibung: | Online Resource |
| ISSN: | 1754-8411 |
| DOI: | 10.1242/dmm.036145 |