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FMN reduces Amyloid...
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Chen, Xin,1980Chalmers tekniska högskola,Chalmers University of Technology
(author)
FMN reduces Amyloid-beta toxicity in yeast by regulating redox status and cellular metabolism
- Article/chapterEnglish2020
Publisher, publication year, extent ...
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2020-02-13
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Springer Science and Business Media LLC,2020
Numbers
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LIBRIS-ID:oai:gup.ub.gu.se/293174
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https://gup.ub.gu.se/publication/293174URI
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https://doi.org/10.1038/s41467-020-14525-4DOI
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https://research.chalmers.se/publication/515586URI
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
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Alzheimer's disease (AD) is defined by progressive neurodegeneration, with oligomerization and aggregation of amyloid-beta peptides (A beta) playing a pivotal role in its pathogenesis. In recent years, the yeast Saccharomyces cerevisiae has been successfully used to clarify the roles of different human proteins involved in neurodegeneration. Here, we report a genome-wide synthetic genetic interaction array to identify toxicity modifiers of A beta 42, using yeast as the model organism. We find that FMN1, the gene encoding riboflavin kinase, and its metabolic product flavin mononucleotide (FMN) reduce A beta 42 toxicity. Classic experimental analyses combined with RNAseq show the effects of FMN supplementation to include reducing misfolded protein load, altering cellular metabolism, increasing NADH/(NADH+NAD(+)) and NADPH/(NADPH+NADP(+)) ratios and increasing resistance to oxidative stress. Additionally, FMN supplementation modifies Htt103QP toxicity and alpha-synuclein toxicity in the humanized yeast. Our findings offer insights for reducing cytotoxicity of A beta 42, and potentially other misfolded proteins, via FMN-dependent cellular pathways.Saccharomyces cerevisiae is a model organism to study proteins involved in neurodegeneration. Here, the authors performed a yeast genome-wide synthetic genetic interaction array (SGA) to screen for toxicity modifiers of A beta 42 and identify riboflavin kinase and its metabolic product flavin mononucleotide as modulators that alleviate cellular A beta 42 toxicity, which is supported by further experimental analyses.
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Ji, Boyang,1983Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)boyang
(author)
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Hao, XinxinGothenburg University,Göteborgs universitet,Institutionen för biomedicin,Centrum för åldrande och hälsa (AgeCap),Institute of Biomedicine,Centre for Ageing and Health (Agecap),University of Gothenburg(Swepub:gu)xxinha
(author)
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Li, Xiaowei,1986Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)lixiaow
(author)
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Eisele, FrederikGothenburg University,Göteborgs universitet,Institutionen för biomedicin,Centrum för åldrande och hälsa (AgeCap),Institute of Biomedicine,Centre for Ageing and Health (Agecap),University of Gothenburg
(author)
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Nyström, Thomas,1960Gothenburg University,Göteborgs universitet,Institutionen för biomedicin,Centrum för åldrande och hälsa (AgeCap),Institute of Biomedicine,Centre for Ageing and Health (Agecap),University of Gothenburg(Swepub:gu)xnysth
(author)
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Petranovic Nielsen, Dina,1975Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)dinap
(author)
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Chalmers tekniska högskolaInstitutionen för biomedicin
(creator_code:org_t)
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In:Nature Communications: Springer Science and Business Media LLC11:12041-1723
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Chen, Xin, 1980
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Ji, Boyang, 1983
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Hao, Xinxin
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Eisele, Frederik
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NATURAL SCIENCES
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University of Gothenburg
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Chalmers University of Technology