MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation

Autor: Cristina Batlle, Isabel Calvo, Valentin Iglesias, Cian J. Lynch, Marcos Gil-Garcia, Manuel Serrano, Salvador Ventura

Publikováno v: Communications Biology, Vol 4, Iss 1, Pp 1-15 (2021)

Batlle et al. identify the presence of coiled-coil (CC) domains that overlap with polyQ tracts in human proteins containing prion-like domains (PrLDs). They demonstrate that human MED15 Mediator complex subunit forms homodimers in solution mediated b

Externí odkaz: https://doaj.org/article/2517a586465644e7b440718bfabfa5ee

hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation

Autor: Cristina Batlle, Peiguo Yang, Maura Coughlin, James Messing, Mireia Pesarrodona, Elzbieta Szulc, Xavier Salvatella, Hong Joo Kim, J. Paul Taylor, Salvador Ventura

Publikováno v: Cell Reports, Vol 30, Iss 4, Pp 1117-1128.e5 (2020)

Summary: 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 lac

Externí odkaz: https://doaj.org/article/cc5833f6bb294484ba448e739b6c1e9f

Rational optimization of a transcription factor activation domain inhibitor

Autor: Shaon Basu, Paula Martínez-Cristóbal, Mireia Pesarrodona, Marta Frigolé-Vivas, Michael Lewis, Elzbieta Szulc, C. Adriana Bañuelos, Carolina Sánchez-Zarzalejo, Stasė Bielskutė, Jiaqi Zhu, Karina Pombo-García, Carla Garcia-Cabau, Cristina Batlle, Borja Mateos, Mateusz Biesaga, Albert Escobedo, Lídia Bardia, Xavier Verdaguer, Alessandro Ruffoni, Nasrin R. Mawji, Jun Wang, Teresa Tam, Isabelle Brun-Heath, Salvador Ventura, David Meierhofer, Jesús García, Paul Robustelli, Travis H. Stracker, Marianne D. Sadar, Antoni Riera, Denes Hnisz, Xavier Salvatella

SummaryTranscription factors are among the most attractive therapeutic targets but are considered largely undruggable due to the intrinsically disordered nature of their activation domains. Here we show that the aromatic character of the activation d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::647a49166ea017e1660f5ae923fe0668
https://doi.org/10.1101/2022.08.18.504385

Perfecting prediction of mutational impact on the aggregation propensity of the ALS-associated hnRNPA2 prion-like protein

Autor: Cristina Batlle, Salvador Ventura, Valentin Iglesias, María Rosario Fernández

Publikováno v: FEBS Letters. 591:1966-1971

An increasing number of human proteins are being found to bear a prion-like domain (PrLD) driving the formation of membraneless compartments through liquid-liquid phase separation. Point mutations in these PrLDs promote the transition to an amyloid-l

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2d0bceaede5195b375136f84cce5747
https://doi.org/10.1002/1873-3468.12698

hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation

Autor: Xavier Salvatella, Cristina Batlle, J. Paul Taylor, Elzbieta Szulc, Mireia Pesarrodona, James Messing, Maura Coughlin, Peiguo Yang, Hong Joo Kim, Salvador Ventura

Publikováno v: Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Cell Reports
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
Cell Reports, Vol 30, Iss 4, Pp 1117-1128.e5 (2020)
Recercat. Dipósit de la Recerca de Catalunya
instname

Summary 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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72eb0262531eaad2e37ca2c61c30da08
https://doi.org/10.1016/j.celrep.2019.12.080