Resumen: Amyloid aggregation of α-synuclein (αS) is the hallmark of Parkinson’s disease and other synucleinopathies. Recently, Tau protein, generally associated with Alzheimer’s disease, has been linked to αS pathology and observed to co- localize in αS-rich disease inclusions, although the molecular mechanisms for the co-aggregation of both proteins remain elusive. We report here that αS phase-separates into liquid condensates by electrostatic complex coacerva- tion with positively charged polypeptides such as Tau. Condensates undergo either fast gelation or coalescence followed by slow amyloid aggregation depending on the affinity of αS for the poly-cation and the rate of valence exhaustion of the condensate network. By combining a set of advanced bio- physical techniques, we have been able to characterize αS/Tau liquid-liquid phase separation and identified key factors that lead to the formation of hetero-aggregates containing both proteins in the interior of the liquid protein condensates. Idioma: Inglés DOI: 10.1038/s41467-022-32350-9 Año: 2022 Publicado en: Nature communications 13 (2022), 4586 [16 pp.] ISSN: 2041-1723 Factor impacto JCR: 16.6 (2022) Categ. JCR: MULTIDISCIPLINARY SCIENCES rank: 6 / 73 = 0.082 (2022) - Q1 - T1 Factor impacto CITESCORE: 24.9 - Physics and Astronomy (Q1) - General (Q1) - Chemistry (Q1) - Biochemistry, Genetics and Molecular Biology (Q1)