RNA-binding protein diversity and NLS arginines regulate FUS mixing in mRNA-rich compartments - PubMed
3 hours ago
- #RNA-binding proteins
- #biomolecular condensates
- #neurodegenerative diseases
- Elevated RNA levels and protein chaperone activity are known to prevent aberrant phase separation of RNA-binding proteins (RBPs) like FUS, which is associated with neurodegenerative diseases.
- Increasing the diversity of RBPs in mRNA-rich condensates helps buffer FUS spatial segregation, promoting mixing instead of forming distinct compartments.
- Arginine residues in the nuclear localization signal (NLS) at the C-terminal end of FUS, which are frequently mutated in pathology, regulate FUS interactions with multiple RBPs, influencing mixing in condensates.
- Pathological NLS mutations in FUS may not only affect nuclear import but also alter interactions with partners in mRNA-rich compartments, impacting the onset and progression of FUS-related neurodegenerative diseases.
- The study explores RBP diversity and NLS arginines as regulatory factors in FUS mixing within biomolecular condensates, linking to mechanisms in diseases like ALS.