TRIM28 regulates the nuclear accumulation and toxicity of both alpha-synuclein and tau.
Identifieur interne : 000134 ( PubMed/Curation ); précédent : 000133; suivant : 000135TRIM28 regulates the nuclear accumulation and toxicity of both alpha-synuclein and tau.
Auteurs : Maxime Wc Rousseaux [États-Unis] ; Maria De Haro [États-Unis] ; Cristian A. Lasagna-Reeves [États-Unis] ; Antonia De Maio [États-Unis] ; Jeehye Park [États-Unis] ; Paymaan Jafar-Nejad [États-Unis] ; Ismael Al-Ramahi [États-Unis] ; Ajay Sharma [États-Unis] ; Lauren See [États-Unis] ; Nan Lu [États-Unis] ; Luis Vilanova-Velez [États-Unis] ; Tiemo J. Klisch [États-Unis] ; Thomas F. Westbrook [États-Unis] ; Juan C. Troncoso [États-Unis] ; Juan Botas [États-Unis] ; Huda Y. Zoghbi [États-Unis]Source :
- eLife [ 2050-084X ] ; 2016.
Abstract
Several neurodegenerative diseases are driven by the toxic gain-of-function of specific proteins within the brain. Elevated levels of alpha-synuclein (α-Syn) appear to drive neurotoxicity in Parkinson's disease (PD); neuronal accumulation of tau is a hallmark of Alzheimer's disease (AD); and their increased levels cause neurodegeneration in humans and model organisms. Despite the clinical differences between AD and PD, several lines of evidence suggest that α-Syn and tau overlap pathologically. The connections between α-Syn and tau led us to ask whether these proteins might be regulated through a shared pathway. We therefore screened for genes that affect post-translational levels of α-Syn and tau. We found that TRIM28 regulates α-Syn and tau levels and that its reduction rescues toxicity in animal models of tau- and α-Syn-mediated degeneration. TRIM28 stabilizes and promotes the nuclear accumulation and toxicity of both proteins. Intersecting screens across comorbid proteinopathies thus reveal shared mechanisms and therapeutic entry points.
DOI: 10.7554/eLife.19809
PubMed: 27779468
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<front><div type="abstract" xml:lang="en">Several neurodegenerative diseases are driven by the toxic gain-of-function of specific proteins within the brain. Elevated levels of alpha-synuclein (α-Syn) appear to drive neurotoxicity in Parkinson's disease (PD); neuronal accumulation of tau is a hallmark of Alzheimer's disease (AD); and their increased levels cause neurodegeneration in humans and model organisms. Despite the clinical differences between AD and PD, several lines of evidence suggest that α-Syn and tau overlap pathologically. The connections between α-Syn and tau led us to ask whether these proteins might be regulated through a shared pathway. We therefore screened for genes that affect post-translational levels of α-Syn and tau. We found that TRIM28 regulates α-Syn and tau levels and that its reduction rescues toxicity in animal models of tau- and α-Syn-mediated degeneration. TRIM28 stabilizes and promotes the nuclear accumulation and toxicity of both proteins. Intersecting screens across comorbid proteinopathies thus reveal shared mechanisms and therapeutic entry points.</div>
</front>
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<ArticleTitle>TRIM28 regulates the nuclear accumulation and toxicity of both alpha-synuclein and tau.</ArticleTitle>
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<Abstract><AbstractText>Several neurodegenerative diseases are driven by the toxic gain-of-function of specific proteins within the brain. Elevated levels of alpha-synuclein (α-Syn) appear to drive neurotoxicity in Parkinson's disease (PD); neuronal accumulation of tau is a hallmark of Alzheimer's disease (AD); and their increased levels cause neurodegeneration in humans and model organisms. Despite the clinical differences between AD and PD, several lines of evidence suggest that α-Syn and tau overlap pathologically. The connections between α-Syn and tau led us to ask whether these proteins might be regulated through a shared pathway. We therefore screened for genes that affect post-translational levels of α-Syn and tau. We found that TRIM28 regulates α-Syn and tau levels and that its reduction rescues toxicity in animal models of tau- and α-Syn-mediated degeneration. TRIM28 stabilizes and promotes the nuclear accumulation and toxicity of both proteins. Intersecting screens across comorbid proteinopathies thus reveal shared mechanisms and therapeutic entry points.</AbstractText>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Program in Developmental Biology, Baylor College of Medicine, Houston, Canada.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Park</LastName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>See</LastName>
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<Initials>L</Initials>
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<Author ValidYN="Y"><LastName>Vilanova-Velez</LastName>
<ForeName>Luis</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, United States.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Jan and Dan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, United States.</Affiliation>
</AffiliationInfo>
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<ForeName>Tiemo J</ForeName>
<Initials>TJ</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, United States.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Jan and Dan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, United States.</Affiliation>
</AffiliationInfo>
</Author>
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<ForeName>Thomas F</ForeName>
<Initials>TF</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, United States.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>The Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, United States.</Affiliation>
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</Author>
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<ForeName>Juan C</ForeName>
<Initials>JC</Initials>
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</Author>
<Author ValidYN="Y"><LastName>Botas</LastName>
<ForeName>Juan</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, United States.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Jan and Dan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, United States.</Affiliation>
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<Author ValidYN="Y"><LastName>Zoghbi</LastName>
<ForeName>Huda Y</ForeName>
<Initials>HY</Initials>
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<AffiliationInfo><Affiliation>Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, United States.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Jan and Dan Duncan Neurological Research Institute, Texas Children's Hospital, Houston, United States.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Program in Developmental Biology, Baylor College of Medicine, Houston, Canada.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Howard Hughes Medical Institute, Baylor College of Medicine, Houston, United States.</Affiliation>
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<Month>10</Month>
<Day>25</Day>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Alzheimer's disease</Keyword>
<Keyword MajorTopicYN="N">D. melanogaster</Keyword>
<Keyword MajorTopicYN="N">Parkinson's disease</Keyword>
<Keyword MajorTopicYN="N">human</Keyword>
<Keyword MajorTopicYN="N">mouse</Keyword>
<Keyword MajorTopicYN="N">neurodegeneration</Keyword>
<Keyword MajorTopicYN="N">neuroscience</Keyword>
<Keyword MajorTopicYN="N">synucleinopathies</Keyword>
<Keyword MajorTopicYN="N">tauopathies</Keyword>
</KeywordList>
<CoiStatement>HYZ: Senior editor, eLife. The other authors declare that no competing interests exist.</CoiStatement>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>07</Month>
<Day>20</Day>
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<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
<Month>10</Month>
<Day>12</Day>
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<PubMedPubDate PubStatus="pubmed"><Year>2016</Year>
<Month>10</Month>
<Day>26</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<Month>10</Month>
<Day>26</Day>
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<ArticleId IdType="pmc">PMC5104516</ArticleId>
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