A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

By Hyun O. Lee, L. Jawerth, Shovamayee Maharana, Marcus Jahnel, Marco Y. Hein, S. Stoynov, J. Mahamid, Shambaditya Saha, Titus M. Franzmann, Andrej Pozniakovski and 9 more. Cell, 2015

2,658 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Neurology

View Paper: https://www.semanticscholar.org/paper/e9dbcb89468f1f3e5256800db63cac6692b220a9

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Citations in the corpus

The Centrosome Is a Selective Condensate that Nucleates Microtubules by Concentrating Tubulin. (2017, background): “Ribonucleoprotein granules, FUS, and nucleoporins mediate interactions through disordered, low-complexity domains and interactions with RNA molecules (Frey and Görlich, 2007; Kato et al., 2012; Patel et al., 2015).”
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis (2019, background): “Phase-separated droplets of the ALS-linked FUS mutants were found to display a propensity to mature into amyloid-like fibrillar aggregates (Patel et al., 2015).”
Stress-triggered phase separation is an adaptive, evolutionarily tuned response (2017, background): “Multivalent interactions between LCRs can suffice to cause liquid-liquid phase separation, amyloid formation, and other demixing phenomena in vitro (Boke et al., 2016; Kato et al., 2012; Lin et al., 2015; Molliex et al., 2015; Patel et al., 2015).”
Liquid-Liquid Phase Separation in Disease. (2019, background): “that promote protein phase separation are often mutated in diseases and promote a rapid conversion of dense protein solutions to protein aggregates (37, 101, 105, 108, 123).”
Hexanediol: a chemical probe to investigate the material properties of membrane-less compartments (2017, methodology): “Understanding the link between the physical properties of membrane-less compartments and their function is of utmost importance, also because transitions into more solid-like states have been linked to age-related diseases [3] [4].”
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits (2016, background): “…composed of hundreds of proteins and RNAs, show dynamic behavior (Kedersha et al., 2005; Bley et al., 2015) compatible with the LLPS model but also may exhibit aberrant transition to more static and solid-like states, as seen in neurodegeneration-associated protein inclusions (Patel et al., 2015).”
Spatiotemporal control of intracellular phase transitions using light-activated optoDroplets (2016, neutral): “While the self-associating N-terminal IDR of FUS has been shown to be necessary and sufficient for liquid-liquid phase separation (Patel et al., 2015), C-terminal RNA binding domains appear to further promote phase separation ((Burke et al., 2015), (Lin et al., 2015)).”
Pi-Pi contacts are an overlooked protein feature relevant to phase separation (2018, positive): “Thus, this represents a valuable tool for the currently expanding field of protein phase separation and its link to biological function and disease (Mitrea and Kriwacki, 2016; Conicella et al., 2016; Patel et al., 2015).”
Phase separation in biology; functional organization of a higher order (2016, methodology): “Alterations in the morphology and viscoelastic properties of mRNP granules, due to mutations in resident proteins (e.g. hnRNPA1, FUS) are associated with debilitating neurodegenerative diseases [13, 42, 44, 45].”
Phase separation of a yeast prion protein promotes cellular fitness (2018, background): “Such meshwork has not been seen in droplets formed by well-described stress and P granule proteins (3, 19).”
Structured states of disordered proteins from genomic sequences (2016, neutral): “Most recently, low complexity sequences have also been associated with physiological prion-like polymers that form hydrogels and membrane-less compartments, such as Fus and hnRNPA2 (Hyman et al., 2014; Kato et al., 2012; Kwon et al., 2013; Patel et al., 2015).”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “of the fused in sarcoma (FUS) RNA-binding protein with RNA [213]; polymerization of mutant FUS forms associated with amyotrophic lateral sclerosis [215]; RNA-dependent hydrogel formation of the LC domains of RBM3, hnRNPA1, hnRNPA2, CIRBP, and the yeast Sup35 protein [213, 216]; RNA-dependent hydroge”