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Decoding and recoding phase behavior of TDP43 reveals that phase separation is not required for splicing function

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/ana.21154openalex-snapshot

TDP‐43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease

inferredcites →https://doi.org/10.1002/anie.201703191openalex-snapshot

Reentrant Phase Transition Drives Dynamic Substructure Formation in Ribonucleoprotein Droplets

inferredcites →https://doi.org/10.1016/bs.adgen.2015.07.001openalex-snapshot

Functional Significance of TDP-43 Mutations in Disease

inferredcites →https://doi.org/10.1016/j.bbapap.2013.01.003openalex-snapshot

Protein disorder, prion propensities, and self-organizing macromolecular collectives

inferredcites →https://doi.org/10.1016/j.bbrc.2006.10.093openalex-snapshot

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1016/j.cell.2015.07.047openalex-snapshot

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

inferredcites →https://doi.org/10.1016/j.cell.2015.09.015openalex-snapshot

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

inferredcites →https://doi.org/10.1016/j.cell.2015.10.040openalex-snapshot

The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei

inferredcites →https://doi.org/10.1016/j.cell.2017.02.007openalex-snapshot

A Phase Separation Model for Transcriptional Control

inferredcites →https://doi.org/10.1016/j.cell.2017.02.027openalex-snapshot

Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response

inferredcites →https://doi.org/10.1016/j.cell.2017.06.022openalex-snapshot

Splicing Activation by Rbfox Requires Self-Aggregation through Its Tyrosine-Rich Domain

inferredcites →https://doi.org/10.1016/j.cell.2017.08.048openalex-snapshot

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains

inferredcites →https://doi.org/10.1016/j.cell.2018.03.056openalex-snapshot

FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions

inferredcites →https://doi.org/10.1016/j.cell.2018.06.006openalex-snapshot

A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins

inferredcites →https://doi.org/10.1016/j.celrep.2016.06.088openalex-snapshot

In Vivo Formation of Vacuolated Multi-phase Compartments Lacking Membranes

inferredcites →https://doi.org/10.1016/j.celrep.2018.06.070openalex-snapshot

Molecular Dissection of FUS Points at Synergistic Effect of Low-Complexity Domains in Toxicity

inferredcites →https://doi.org/10.1016/j.cis.2010.10.003openalex-snapshot

Coacervation of tropoelastin

inferredcites →https://doi.org/10.1016/j.jmb.2005.02.038openalex-snapshot

Human, Drosophila, and C.elegans TDP43: Nucleic Acid Binding Properties and Splicing Regulatory Function

inferredcites →https://doi.org/10.1016/j.molcel.2015.08.018openalex-snapshot

Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins

inferredcites →https://doi.org/10.1016/j.molcel.2016.05.042openalex-snapshot

Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein

inferredcites →https://doi.org/10.1016/j.molcel.2018.07.002openalex-snapshot

Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization

inferredcites →https://doi.org/10.1016/j.neuron.2015.10.030openalex-snapshot

ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function

inferredcites →https://doi.org/10.1016/j.str.2016.07.007openalex-snapshot

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain

inferredcites →https://doi.org/10.1016/j.tcb.2016.05.004openalex-snapshot

Principles and Properties of Stress Granules

inferredcites →https://doi.org/10.1016/j.tibs.2017.12.001openalex-snapshot

Paraspeckles: Where Long Noncoding RNA Meets Phase Separation

inferredcites →https://doi.org/10.1016/s0006-3495(98)77529-0openalex-snapshot

A Helix Propensity Scale Based on Experimental Studies of Peptides and Proteins

inferredcites →https://doi.org/10.1021/acs.biochem.7b01136openalex-snapshot

Functional Implications of Intracellular Phase Transitions

inferredcites →https://doi.org/10.1021/acs.biochem.8b00008openalex-snapshot

Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions

inferredcites →https://doi.org/10.1038/emboj.2012.251openalex-snapshot

Alternative 3′‐end processing of long noncoding RNA initiates construction of nuclear paraspeckles

inferredcites →https://doi.org/10.1038/emboj.2012.302openalex-snapshot

Systematic analysis of barrier‐forming FG hydrogels from Xenopus nuclear pore complexes

inferredcites →https://doi.org/10.1038/nature22038openalex-snapshot

Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice

inferredcites →https://doi.org/10.1038/nature22822openalex-snapshot

Liquid droplet formation by HP1α suggests a role for phase separation in heterochromatin

inferredcites →https://doi.org/10.1038/nature22989openalex-snapshot

Phase separation drives heterochromatin domain formation

inferredcites →https://doi.org/10.1038/ng.132openalex-snapshot

TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1038/nn.2778openalex-snapshot

Characterizing the RNA targets and position-dependent splicing regulation by TDP-43

inferredcites →https://doi.org/10.1038/nn.2779openalex-snapshot

Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

inferredcites →https://doi.org/10.1038/nprot.2013.143openalex-snapshot

Genome engineering using the CRISPR-Cas9 system

inferredcites →https://doi.org/10.1038/nrm.2017.7openalex-snapshot

Biomolecular condensates: organizers of cellular biochemistry

inferredcites →https://doi.org/10.1038/nsmb.2698openalex-snapshot

Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

inferredcites →https://doi.org/10.1038/s41467-017-00062-0openalex-snapshot

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

inferredcites →https://doi.org/10.1038/s41594-018-0050-8openalex-snapshot

Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation

inferredcites →https://doi.org/10.1038/s41594-018-0064-2openalex-snapshot

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation

inferredcites →https://doi.org/10.1073/pnas.0900688106openalex-snapshot

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

inferredcites →https://doi.org/10.1073/pnas.1211577110openalex-snapshot

Misregulation of human sortilin splicing leads to the generation of a nonfunctional progranulin receptor

inferredcites →https://doi.org/10.1073/pnas.1222809110openalex-snapshot

ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43

inferredcites →https://doi.org/10.1073/pnas.1614462114openalex-snapshot

Amyotrophic lateral sclerosis-linked mutations increase the viscosity of liquid-like TDP-43 RNP granules in neurons

inferredcites →https://doi.org/10.1073/pnas.1706197114openalex-snapshot

Structural and hydrodynamic properties of an intrinsically disordered region of a germ cell-specific protein on phase separation

inferredcites →https://doi.org/10.1073/pnas.212483099openalex-snapshot

Higher order arrangement of the eukaryotic nuclear bodies

inferredcites →https://doi.org/10.1074/jbc.ac117.001037openalex-snapshot

TAR DNA-binding protein 43 (TDP-43) liquid–liquid phase separation is mediated by just a few aromatic residues

inferredcites →https://doi.org/10.1074/jbc.m109.010264openalex-snapshot

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

inferredcites →https://doi.org/10.1074/jbc.m111.328757openalex-snapshot

Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)

inferredcites →https://doi.org/10.1074/jbc.m113.463828openalex-snapshot

Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion

inferredcites →https://doi.org/10.1074/jbc.m505557200openalex-snapshot

TDP-43 Binds Heterogeneous Nuclear Ribonucleoprotein A/B through Its C-terminal Tail

inferredcites →https://doi.org/10.1083/jcb.201504117openalex-snapshot

Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles

inferredcites →https://doi.org/10.1083/jcb.201601071openalex-snapshot

Structural, super-resolution microscopy analysis of paraspeckle nuclear body organization

inferredcites →https://doi.org/10.1093/emboj/20.7.1774openalex-snapshot

Nuclear factor TDP‐43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping

inferredcites →https://doi.org/10.1093/nar/gkp342openalex-snapshot

Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo

inferredcites →https://doi.org/10.1093/nar/gkx460openalex-snapshot

Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding

inferredcites →https://doi.org/10.1111/febs.13651openalex-snapshot

The TDP‐43 N‐terminal domain structure at high resolution

inferredcites →https://doi.org/10.1111/j.1471-4159.2009.06383.xopenalex-snapshot

TDP‐43 is recruited to stress granules in conditions of oxidative insult

inferredcites →https://doi.org/10.1126/science.1134108openalex-snapshot

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/science.1154584openalex-snapshot

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/science.1247005openalex-snapshot

Genome-Scale CRISPR-Cas9 Knockout Screening in Human Cells

inferredcites →https://doi.org/10.1126/science.aab0983openalex-snapshot

TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD

inferredcites →https://doi.org/10.1126/science.aan6398openalex-snapshot

Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks

inferredcites →https://doi.org/10.1126/science.aar7366openalex-snapshot

RNA buffers the phase separation behavior of prion-like RNA binding proteins

inferredcites →https://doi.org/10.1128/mcb.01279-10openalex-snapshot

TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor

inferredcites →https://doi.org/10.1136/jmg.2010.077180openalex-snapshot

SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: genotype–phenotype correlations

inferredcites →https://doi.org/10.1186/s40478-018-0586-1openalex-snapshot

Nuclear poly(ADP-ribose) activity is a therapeutic target in amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1242/jcs.200295openalex-snapshot

The wisdom of crowds: regulating cell function through condensed states of living matter

inferredcites →https://doi.org/10.1371/journal.pbio.1002338openalex-snapshot

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43

inferredcites →https://doi.org/10.1371/journal.pone.0006529openalex-snapshot

A Versatile Viral System for Expression and Depletion of Proteins in Mammalian Cells

inferredcites →https://doi.org/10.7554/elife.04251openalex-snapshot

Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity

inferredcites →https://doi.org/10.7554/elife.31486openalex-snapshot

Pi-Pi contacts are an overlooked protein feature relevant to phase separation

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1038/s41467-019-12101-zopenalex-snapshot

The mutational landscape of a prion-like domain

inferred← citeshttps://doi.org/10.1093/nar/gkab582openalex-snapshot

The phase separation-dependent FUS interactome reveals nuclear and cytoplasmic function of liquid–liquid phase separation

inferred← citeshttps://doi.org/10.21203/rs.3.rs-2200020/v1openalex-snapshot

A TDP-43 acetylation-mimic mutation that disrupts RNA-binding drives FTLD-like neurodegeneration in a mouse model of sporadic TDP-43 proteinopathy

inferred← citeshttps://doi.org/10.21203/rs.3.rs-2200020/v2openalex-snapshot