Francelle, Laetitia

[["dc.bibliographiccitation.artnumber","17"],["dc.bibliographiccitation.journal","Frontiers in Human Neuroscience"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Francelle, Laetitia"],["dc.contributor.author","Lotz, Caroline"],["dc.contributor.author","Outeiro, Tiago"],["dc.contributor.author","Brouillet, Emmanuel"],["dc.contributor.author","Merienne, Karine"],["dc.date.accessioned","2018-11-07T10:28:14Z"],["dc.date.available","2018-11-07T10:28:14Z"],["dc.date.issued","2017"],["dc.description.abstract","Unbalanced epigenetic regulation is thought to contribute to the progression of several neurodegenerative diseases, including Huntington's disease (HD), a genetic disorder considered as a paradigm of epigenetic dysregulation. In this review, we attempt to address open questions regarding the role of epigenetic changes in HD, in the light of recent advances in neuroepigenetics. We particularly discuss studies using genome-wide scale approaches that provide insights into the relationship between epigenetic regulations, gene expression and neuronal activity in normal and diseased neurons, including HD neurons. We propose that cell-type specific techniques and 3D based methods will advance knowledge of epigenome in the context of brain region vulnerability in neurodegenerative diseases. A better understanding of the mechanisms underlying epigenetic changes and of their consequences in neurodegenerative diseases is required to design therapeutic strategies more effective than current strategies based on histone deacetylase (HDAC) inhibitors. Researches in HD may play a driving role in this process."],["dc.identifier.doi","10.3389/fnhum.2017.00017"],["dc.identifier.isi","000392986400001"],["dc.identifier.pmid","28194101"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14318"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43381"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Frontiers Media Sa"],["dc.relation.issn","1662-5161"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Contribution of Neuroepigenetics to Huntington's Disease"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","76"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Human Molecular Genetics"],["dc.bibliographiccitation.lastpage","85"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Blum, David"],["dc.contributor.author","Herrera, Federico"],["dc.contributor.author","Francelle, Laetitia"],["dc.contributor.author","Mendes, Tiago"],["dc.contributor.author","Basquin, Marie"],["dc.contributor.author","Obriot, Helene"],["dc.contributor.author","Demeyer, Dominique"],["dc.contributor.author","Sergeant, Nicolas"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Brouillet, Emmanuel"],["dc.contributor.author","Buée, Luc"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.date.accessioned","2018-11-07T10:03:30Z"],["dc.date.available","2018-11-07T10:03:30Z"],["dc.date.issued","2015"],["dc.description.abstract","Tau abnormalities play a central role in several neurodegenerative diseases, collectively known as tauopathies. In the present study, we examined whether mutant huntingtin (mHtt), which causes Huntington's disease (HD), modifies Tau phosphorylation and subcellular localization using cell and mouse HD models. Initially, we used novel bimolecular fluorescence complementation assays in live cells to evaluate Tau interactions with either wild type (25QHtt) ormutant huntingtin(103QHtt). While 25QHtt and Tau interacted at the level of the microtubule network, 103QHtt and Tau interacted and formed 'ring-like' inclusions localized in the vicinity of the microtubular organizing center (MTOC). Fluorescence recovery after photobleaching experiments also indicated that, whereas homomeric 103QHtt/103QHtt pairs rapidly re-entered into inclusions, heteromeric 103QHtt/Tau pairs remained excluded from the 'ring-like' inclusions. Interestingly, in vitro Tau relocalization was associated to Tau hyperphosphorylation. Consistent with this observation, we found strong Tau hyperphosphorylation in brain samples from two different mouse models of HD, R6/2 and 140CAG knock-in. This was associated with a significant reduction in the levels of Tau phosphatases (PP1, PP2A and PP2B), with no apparent involvement of major Tau kinases. Thus, the present study strongly suggests that expression of mHtt leads to Tau hyperphosphorylation, relocalization and sequestration through direct protein-protein interactions in inclusion-like compartments in the vicinity of the MTOC. Likewise, our data also suggest that Tau alterations may also contribute to HD pathogenesis."],["dc.identifier.doi","10.1093/hmg/ddu421"],["dc.identifier.isi","000350135400007"],["dc.identifier.pmid","25143394"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38481"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1460-2083"],["dc.relation.issn","0964-6906"],["dc.title","Mutant huntingtin alters Tau phosphorylation and subcellular distribution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]