TY - JOUR
T1 - Dataset on the effect of Rubicon overexpression on polyglutamine-induced locomotor dysfunction in Drosophila
AU - Oba, Masaki
AU - Fukui, Koji
AU - Sango, Kazunori
AU - Suzuki, Mari
N1 - Funding Information:
This work was supported in part by Grant-in-Aid for JSPS Fellows ( 20J22554 to M.O.); Grant-in-Aid for Scientific Research (C) ( 19K07987 to M.S.) from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT), Japan; by Research Grants from Takeda Science Foundation (to M.S.); by Research Grants from The Mochida Memorial Foundation for Medical and Pharmaceutical Research (to M.S.).
Publisher Copyright:
© 2021
PY - 2021/8
Y1 - 2021/8
N2 - The accumulation of pathogenic misfolded proteins is believed to be a common mechanism of generation of neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and polyglutamine (polyQ) diseases. The autophagy–lysosome degradation system has been considered as a potential therapeutic target against these disorders, as it is able to degrade large protein aggregates. Previously, we focused on Rubicon, a negative regulator of autophagy, and demonstrated that knockdown of the Drosophila homolog of Rubicon (dRubicon) suppressed locomotor dysfunction in a fly model of polyQ disease. This suppression was associated with increased autophagic activity and a marked reduction in the number of polyQ inclusion bodies [1]. We generated transgenic fly lines expressing hemagglutinin-tagged dRubicon wild-type (WT) or dRubicon in which the RUN [after RPIP8 (RaP2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus)] domain was deleted (ΔRUN). We provide data regarding the effect of WT and ΔRUN dRubicon co-expression on polyQ-induced locomotor dysfunction in Drosophila.
AB - The accumulation of pathogenic misfolded proteins is believed to be a common mechanism of generation of neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and polyglutamine (polyQ) diseases. The autophagy–lysosome degradation system has been considered as a potential therapeutic target against these disorders, as it is able to degrade large protein aggregates. Previously, we focused on Rubicon, a negative regulator of autophagy, and demonstrated that knockdown of the Drosophila homolog of Rubicon (dRubicon) suppressed locomotor dysfunction in a fly model of polyQ disease. This suppression was associated with increased autophagic activity and a marked reduction in the number of polyQ inclusion bodies [1]. We generated transgenic fly lines expressing hemagglutinin-tagged dRubicon wild-type (WT) or dRubicon in which the RUN [after RPIP8 (RaP2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus)] domain was deleted (ΔRUN). We provide data regarding the effect of WT and ΔRUN dRubicon co-expression on polyQ-induced locomotor dysfunction in Drosophila.
KW - Autophagy
KW - Drosophila melanogaster
KW - Machado–Joseph disease
KW - Polyglutamine
KW - Spinocerebellar ataxia 3
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U2 - 10.1016/j.dib.2021.107222
DO - 10.1016/j.dib.2021.107222
M3 - Article
AN - SCOPUS:85108120697
SN - 2352-3409
VL - 37
JO - Data in Brief
JF - Data in Brief
M1 - 107222
ER -