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dc.contributor.author
Foressi, Nahuel Naum  
dc.contributor.author
Cruz Rodríguez, Leandro  
dc.contributor.author
Celej, Maria Soledad  
dc.date.available
2024-02-07T12:29:24Z  
dc.date.issued
2023-11  
dc.identifier.citation
Foressi, Nahuel Naum; Cruz Rodríguez, Leandro; Celej, Maria Soledad; Heterotypic liquid-liquid phase separation of tau and α-synuclein: Implications for overlapping neuropathologies; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1871; 6; 11-2023; 1-10  
dc.identifier.issn
1570-9639  
dc.identifier.uri
http://hdl.handle.net/11336/226123  
dc.description.abstract
Tauopathies and synucleinopathies are characterized by the aggregation of Tau and α-synuclein (AS) into amyloid structures, respectively. Individuals with these neuropathies have an elevated risk of developing subsequent neurodegenerative or comorbid disorders. Intriguingly, post-mortem brain examinations have revealed co-localization of Tau and AS aggregates, suggesting a synergistic pathological relationship with an adverse prognosis. The role of liquid-liquid phase separation (LLPS) in the development of neurodegenerative diseases is currently receiving significant attention, as it can contribute to the aggregation and co-deposition of amyloidogenic proteins. In this study, we investigated the phase separation behavior of Tau and AS under various insults, some of which are implicated in disease progression. Our findings demonstrate the formation of heterotypic droplets composed of Tau and AS at physiologically relevant mole ratios that mimic neurons' soma and terminal buttons. Importantly, these heterotypic droplets exhibit increased resistance to electrostatic screening compared to homotypic condensates. Moreover, we observed that biologically relevant biomolecules, known to be dysregulated in disease, exert different effects on these droplets. Additionally, we provide evidence that phase separation itself influences the amyloid aggregation of Tau and AS, underscoring the significance of this process in the development of aggregopathies.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/restrictedAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
AMYLOID  
dc.subject
CONDENSATES  
dc.subject
LIQUID-LIQUID PHASE SEPARATION  
dc.subject
MICROSCOPY  
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PROTEIN AGGREGATION  
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SYNUCLEIN  
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TAU PROTEIN  
dc.subject.classification
Biofísica  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Heterotypic liquid-liquid phase separation of tau and α-synuclein: Implications for overlapping neuropathologies  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2024-02-06T13:30:36Z  
dc.journal.volume
1871  
dc.journal.number
6  
dc.journal.pagination
1-10  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Foressi, Nahuel Naum. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina  
dc.description.fil
Fil: Cruz Rodríguez, Leandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina  
dc.description.fil
Fil: Celej, Maria Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina  
dc.journal.title
Biochimica Et Biophysica Acta-proteins And Proteomics  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S157096392300064X  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbapap.2023.140950