Direct α-synuclein promoter transactivation by the tumor suppressor p53
Identifieur interne : 000302 ( Main/Curation ); précédent : 000301; suivant : 000303Direct α-synuclein promoter transactivation by the tumor suppressor p53
Auteurs : Eric Duplan ; Cécile Giordano ; Frédéric Checler ; Cristine Alves Da CostaSource :
- Molecular Neurodegeneration [ 1750-1326 ] ; 2016.
English descriptors
- KwdEn :
- Animals, Brain (metabolism), Dopaminergic Neurons (metabolism), Gene Expression Regulation (genetics), Lewy Bodies (metabolism), Mice, Knockout, Parkinson Disease (genetics), Promoter Regions, Genetic, Substantia Nigra (metabolism), Substantia Nigra (pathology), Transcriptional Activation (genetics), Tumor Suppressor Protein p53 (metabolism), Up-Regulation, alpha-Synuclein (metabolism).
- MESH :
- chemical , metabolism : Tumor Suppressor Protein p53, alpha-Synuclein.
- genetics : Gene Expression Regulation, Parkinson Disease, Transcriptional Activation.
- metabolism : Brain, Dopaminergic Neurons, Lewy Bodies, Substantia Nigra.
- pathology : Substantia Nigra.
- Animals, Mice, Knockout, Promoter Regions, Genetic, Up-Regulation.
Abstract
Parkinson’s disease (PD) is a motor disease associated with the degeneration of dopaminergic neurons of the
We show that pharmacological and genetic up-regulation of p53 expression lead to a strong increase of α-synuclein protein, promoter activity and mRNA levels. Several lines of evidence indicate that this transcriptional control is due to the DNA-binding properties of p53. Firstly, p53 DNA-binding dead mutations abolish p53 regulation of α-synuclein. Secondly, the deletion of p53 responsive element from α-synuclein promoter abrogates p53-mediated α-synuclein regulation. Thirdly, gel shift and chromatin immunoprecipitation studies indicate that p53 interacts physically with α-synuclein promoter both in vitro and in a physiological context. Furthermore, we show that the depletion of endogenous p53 in cells as well as in knockout mice down-regulates α-synuclein transcription.
Overall, we have identified α-synuclein as a new transcriptional target of p53 and delineated a cellular mechanism feeding the accumulation of toxic aggregated α-synuclein in PD. This original α-syn regulatory mechanism may be central to PD-related cell death and may lead to novel opportunities to design alternative neuroprotective strategies in PD.
The online version of this article (doi:10.1186/s13024-016-0079-2) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1186/s13024-016-0079-2
PubMed: 26833254
PubMed Central: 4736712
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Eric Duplan<affiliation><nlm:aff id="Aff1">Institut de Pharmacologie Moléculaire et Cellulaire, UMR7275 CNRS/UNSA, team labeled “Fondation pour la Recherche Médicale” and “Laboratory of Excellence (LABEX) Distalz”, 660 route des Lucioles, 06560 Sophia-Antipolis, Valbonne France</nlm:aff>
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<series><title level="j">Molecular Neurodegeneration</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Brain (metabolism)</term>
<term>Dopaminergic Neurons (metabolism)</term>
<term>Gene Expression Regulation (genetics)</term>
<term>Lewy Bodies (metabolism)</term>
<term>Mice, Knockout</term>
<term>Parkinson Disease (genetics)</term>
<term>Promoter Regions, Genetic</term>
<term>Substantia Nigra (metabolism)</term>
<term>Substantia Nigra (pathology)</term>
<term>Transcriptional Activation (genetics)</term>
<term>Tumor Suppressor Protein p53 (metabolism)</term>
<term>Up-Regulation</term>
<term>alpha-Synuclein (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Tumor Suppressor Protein p53</term>
<term>alpha-Synuclein</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Gene Expression Regulation</term>
<term>Parkinson Disease</term>
<term>Transcriptional Activation</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term>
<term>Dopaminergic Neurons</term>
<term>Lewy Bodies</term>
<term>Substantia Nigra</term>
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<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Substantia Nigra</term>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>Parkinson’s disease (PD) is a motor disease associated with the degeneration of dopaminergic neurons of the <italic>substantia nigra pars compacta</italic>
. p53 is a major neuronal pro-apoptotic factor that is at the center of gravity of multiple physiological and pathological cascades, some of which implying several key PD-linked proteins. Since p53 is up-regulated in PD-affected brain, we have examined its ability to regulate the transcription of α-synuclein, a key protein that accumulates in PD-related Lewy bodies.</p>
</sec>
<sec><title>Results</title>
<p>We show that pharmacological and genetic up-regulation of p53 expression lead to a strong increase of α-synuclein protein, promoter activity and mRNA levels. Several lines of evidence indicate that this transcriptional control is due to the DNA-binding properties of p53. Firstly, p53 DNA-binding dead mutations abolish p53 regulation of α-synuclein. Secondly, the deletion of p53 responsive element from α-synuclein promoter abrogates p53-mediated α-synuclein regulation. Thirdly, gel shift and chromatin immunoprecipitation studies indicate that p53 interacts physically with α-synuclein promoter both in vitro and in a physiological context. Furthermore, we show that the depletion of endogenous p53 in cells as well as in knockout mice down-regulates α-synuclein transcription.</p>
</sec>
<sec><title>Conclusions</title>
<p>Overall, we have identified α-synuclein as a new transcriptional target of p53 and delineated a cellular mechanism feeding the accumulation of toxic aggregated α-synuclein in PD. This original α-syn regulatory mechanism may be central to PD-related cell death and may lead to novel opportunities to design alternative neuroprotective strategies in PD.</p>
</sec>
<sec><title>Electronic supplementary material</title>
<p>The online version of this article (doi:10.1186/s13024-016-0079-2) contains supplementary material, which is available to authorized users.</p>
</sec>
</div>
</front>
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<author><name sortKey="Schlaudraff, F" uniqKey="Schlaudraff F">F Schlaudraff</name>
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<author><name sortKey="Konopka, T" uniqKey="Konopka T">T Konopka</name>
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<author><name sortKey="Chen, D" uniqKey="Chen D">D Chen</name>
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<author><name sortKey="Giordano, C" uniqKey="Giordano C">C Giordano</name>
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