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18 p, 3.6 MB hnRNPDL phase separation is regulated by alternative splicing and disease-causing mutations accelerate its aggregation / Batlle Carreras, Cristina (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Yang, Peiguo (St. Jude Children's Research Hospital (Memphis, Estats Units d'Amèrica)) ; Coughlin, Maura (St. Jude Children's Research Hospital (Memphis, Estats Units d'Amèrica)) ; Messing, James (Howard Hughes Medical Institute) ; Pesarrodona Roches, Mireia (Institut de Recerca Biomèdica de Lleida) ; Szulc, Elzbieta (Institut de Recerca Biomèdica de Lleida) ; Salvatella, Xavier (Institut de Recerca Biomèdica de Lleida) ; Kim, Hong Joo (St. Jude Children's Research Hospital (Memphis, Estats Units d'Amèrica)) ; Taylor, J. Paul (Howard Hughes Medical Institute) ; Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Prion-like proteins form multivalent assemblies and phase separate into membraneless organelles. Heterogeneous ribonucleoprotein D-like (hnRNPDL) is a RNA-processing prion-like protein with three alternative splicing (AS) isoforms, which lack none, one, or both of its two disordered domains. [...]
2020 - 10.1016/j.celrep.2019.12.080
Cell reports, Vol. 30, issue 4 (Jan. 2020) , p. 1117-1128  

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