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Peer-Reviewed Publication
Cell Rep2026;45(6):117430.June 23, 2026Journal Article

RNA-binding protein diversity and NLS arginines regulate FUS mixing in mRNA-rich compartments.

Diane Valenti1, Vandana Joshi2, Serhii Pankivskyi2, Hoang Hung Cai2, Loic Hamon2, Bénédicte Desforges2, Amandine Molliex3, Julien Duez3, Julian Bursztyka4, Laurianne Davignon4, Alexandre Maucuer2, Guillaume Bollot3, David Pastré5
1Université Paris-Saclay, INSERM U1204, University Evry, Structure-Activité des Biomolécules Normales et Pathologiques (SABNP), Evry-Courcouronnes, France; Revvity, 1 Av. de Marne et Gondoire, 77600 Bussy-Saint-Martin, France.
2Université Paris-Saclay, INSERM U1204, University Evry, Structure-Activité des Biomolécules Normales et Pathologiques (SABNP), Evry-Courcouronnes, France.
3IKTOS, 65 rue de Prony, 75017 Paris, France.
4Revvity, 1 Av. de Marne et Gondoire, 77600 Bussy-Saint-Martin, France.
5Université Paris-Saclay, INSERM U1204, University Evry, Structure-Activité des Biomolécules Normales et Pathologiques (SABNP), Evry-Courcouronnes, France. Electronic address: david.pastre@univ-evry.fr.
PubMed DOI

Abstract

Despite being prone to condensation, many RNA-binding proteins (RBPs) do not form large condensates in cells. This issue is still widely researched, particularly because aggregation of RBPs, such as FUS, is the hallmark of some neurodegenerative diseases. Elevated RNA levels and protein chaperone activity have already emerged as key factors preventing aberrant phase separation. Here, we explored t…

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