ArticleProtein science : a publication of the Protein Society2022
The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA-binding proteins for liquid-liquid phase separation.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 32 citations in OpenAlex.
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- Molecular mechanisms mediated by liquid-liquid phase separation in chronic liver disease progression.iScience · 2025Review
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- Protein language model identifies disordered, conserved motifs implicated in phase separation.eLife · 2025Article
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- A Few Charged Residues in Galectin-3's Folded and Disordered Regions Regulate Phase Separation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- TDP-43 Amyloid Fibril Formation via Phase Separation-Related and -Unrelated Pathways.ACS chemical neuroscience · 2024Article
- Refining the pool of RNA-binding domains advances the classification and prediction of RNA-binding proteins.Nucleic acids research · 2024Article
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- Programmable de novo designed coiled coil-mediated phase separation in mammalian cells.Nature communications · 2023Article
- Hormone-induced enhancer assembly requires an optimal level of hormone receptor multivalent interactions.Molecular cell · 2023Article
- IFF: Identifying key residues in intrinsically disordered regions of proteins using machine learning.Protein science : a publication of the Protein Society · 2023Article
- The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA-binding proteins for liquid-liquid phase separation.Protein science : a publication of the Protein Society · 2022Article
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2 authors at 1 institution in 1 country.
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Abstract
Aromatic residues appeared relatively late in the evolution of protein sequences to stabilize the globular proteins' folding core and are less in the intrinsically disordered regions (IDRs). Recent advances in protein liquid-liquid phase separation (LLPS) studies have also shown that aromatic residues in IDRs often act as "stickers" to promote multivalent interactions in forming higher-order oligomers. To study how general these structure-promoting residues are in IDRs, we compared levels of sequence disorder in RNA binding proteins (RBPs), which are often found to undergo LLPS, and the human proteome. We found that aromatic residues appear more frequently than expected in the IDRs of RBPs and, through multiple sequence alignment analysis, those aromatic residues are often conserved among chordates. Using TDP-43, FUS, and some other well-studied LLPS proteins as examples, the conserved aromatic residues are important to their LLPS-related functions. These analyses suggest that aromatic residues may have contributed twice to evolution: stabilizing structured proteins and assembling biomolecular condensates.
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