Parkin: much more than a simple ubiquitin ligase.
Identifieur interne : 000911 ( PubMed/Corpus ); précédent : 000910; suivant : 000912Parkin: much more than a simple ubiquitin ligase.
Auteurs : C. Alves Da Costa ; F. CheclerSource :
- Neuro-degenerative diseases [ 1660-2862 ] ; 2012.
English descriptors
- KwdEn :
- Animals, Brain (metabolism), Cell Death (genetics), Humans, Mice, Mutation (genetics), Parkinson Disease (genetics), Parkinson Disease (metabolism), Parkinson Disease (pathology), Tumor Suppressor Protein p53 (genetics), Tumor Suppressor Protein p53 (metabolism), Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism).
- MESH :
- chemical , genetics : Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases.
- genetics : Cell Death, Mutation, Parkinson Disease.
- metabolism : Brain, Parkinson Disease, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases.
- pathology : Parkinson Disease.
- Animals, Humans, Mice.
Abstract
Parkin is mainly a cytosolic protein involved in a subset of Parkinson's disease (PD) cases referred to as autosomal juvenile recessive forms of PD. Most studies have established as a dogma that parkin function could be resumed as an ubiquitin ligase activity. Accordingly, several cellular functions ascribed to parkin derive from its ability to ubiquitinate a series of proteins, thereby rendering them prone to proteasomal degradation. Several lines of data indicated that parkin could display antiapoptotic properties and we demonstrated that indeed, parkin could downregulate the p53-dependent pathway. However, we showed that such function remained independent of parkin's ability to act as an ubiquitin ligase. Thus, we established that parkin repressed p53 transcription by physically interacting with its promoter. Here, we describe this novel parkin-associated transcription factor function and we speculate on putative additional transcriptional targets.
DOI: 10.1159/000332803
PubMed: 22204976
Links to Exploration step
pubmed:22204976Le document en format XML
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<author><name sortKey="Alves Da Costa, C" sort="Alves Da Costa, C" uniqKey="Alves Da Costa C" first="C" last="Alves Da Costa">C. Alves Da Costa</name>
<affiliation><nlm:affiliation>Institut de Pharmacologie Moléculaire et Cellulaire et Institut de NeuroMédecine Moléculaire, Equipe Labellisée Fondation pour la Recherche Médicale, Sophia-Antipolis, Valbonne, France.</nlm:affiliation>
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<author><name sortKey="Checler, F" sort="Checler, F" uniqKey="Checler F" first="F" last="Checler">F. Checler</name>
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<affiliation><nlm:affiliation>Institut de Pharmacologie Moléculaire et Cellulaire et Institut de NeuroMédecine Moléculaire, Equipe Labellisée Fondation pour la Recherche Médicale, Sophia-Antipolis, Valbonne, France.</nlm:affiliation>
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<series><title level="j">Neuro-degenerative diseases</title>
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<term>Mice</term>
<term>Mutation (genetics)</term>
<term>Parkinson Disease (genetics)</term>
<term>Parkinson Disease (metabolism)</term>
<term>Parkinson Disease (pathology)</term>
<term>Tumor Suppressor Protein p53 (genetics)</term>
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<term>Ubiquitin-Protein Ligases (genetics)</term>
<term>Ubiquitin-Protein Ligases (metabolism)</term>
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<term>Ubiquitin-Protein Ligases</term>
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<term>Mutation</term>
<term>Parkinson Disease</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term>
<term>Parkinson Disease</term>
<term>Tumor Suppressor Protein p53</term>
<term>Ubiquitin-Protein Ligases</term>
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<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinson Disease</term>
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<front><div type="abstract" xml:lang="en">Parkin is mainly a cytosolic protein involved in a subset of Parkinson's disease (PD) cases referred to as autosomal juvenile recessive forms of PD. Most studies have established as a dogma that parkin function could be resumed as an ubiquitin ligase activity. Accordingly, several cellular functions ascribed to parkin derive from its ability to ubiquitinate a series of proteins, thereby rendering them prone to proteasomal degradation. Several lines of data indicated that parkin could display antiapoptotic properties and we demonstrated that indeed, parkin could downregulate the p53-dependent pathway. However, we showed that such function remained independent of parkin's ability to act as an ubiquitin ligase. Thus, we established that parkin repressed p53 transcription by physically interacting with its promoter. Here, we describe this novel parkin-associated transcription factor function and we speculate on putative additional transcriptional targets.</div>
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<DateCompleted><Year>2012</Year>
<Month>08</Month>
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<DateRevised><Year>2016</Year>
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<JournalIssue CitedMedium="Internet"><Volume>10</Volume>
<Issue>1-4</Issue>
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<Title>Neuro-degenerative diseases</Title>
<ISOAbbreviation>Neurodegener Dis</ISOAbbreviation>
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<ArticleTitle>Parkin: much more than a simple ubiquitin ligase.</ArticleTitle>
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<Abstract><AbstractText>Parkin is mainly a cytosolic protein involved in a subset of Parkinson's disease (PD) cases referred to as autosomal juvenile recessive forms of PD. Most studies have established as a dogma that parkin function could be resumed as an ubiquitin ligase activity. Accordingly, several cellular functions ascribed to parkin derive from its ability to ubiquitinate a series of proteins, thereby rendering them prone to proteasomal degradation. Several lines of data indicated that parkin could display antiapoptotic properties and we demonstrated that indeed, parkin could downregulate the p53-dependent pathway. However, we showed that such function remained independent of parkin's ability to act as an ubiquitin ligase. Thus, we established that parkin repressed p53 transcription by physically interacting with its promoter. Here, we describe this novel parkin-associated transcription factor function and we speculate on putative additional transcriptional targets.</AbstractText>
<CopyrightInformation>Copyright © 2011 S. Karger AG, Basel.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Alves da Costa</LastName>
<ForeName>C</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Institut de Pharmacologie Moléculaire et Cellulaire et Institut de NeuroMédecine Moléculaire, Equipe Labellisée Fondation pour la Recherche Médicale, Sophia-Antipolis, Valbonne, France.</Affiliation>
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<Language>eng</Language>
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