TDP-43 condensation properties specify its RNA-binding and regulatory repertoire
Published 2021 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
TDP-43 condensation properties specify its RNA-binding and regulatory repertoire
Authors
Keywords
RNA-binding protein, TDP-43, iCLIP, condensation, RNA granules, phase separation, intrinsically disordered region, amyotrophic lateral sclerosis, multivalency, alternative polyadenylation
Journal
CELL
Volume 184, Issue 18, Pages 4680-4696.e22
Publisher
Elsevier BV
Online
2021-08-10
DOI
10.1016/j.cell.2021.07.018
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
- (2021) Simon Alberti et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
- (2021) Paraskevi Tziortzouda et al. NATURE REVIEWS NEUROSCIENCE
- Tandem RNA binding sites induce self-association of the stress granule marker protein TIA-1
- (2021) Fionna E Loughlin et al. NUCLEIC ACIDS RESEARCH
- TDP-43 stabilizes G3BP1 mRNA: relevance to amyotrophic lateral sclerosis/frontotemporal dementia
- (2021) Hadjara Sidibé et al. BRAIN
- TDP-43 α-helical structure tunes liquid–liquid phase separation and function
- (2020) Alexander E. Conicella et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Recruitment of mRNAs to P granules by condensation with intrinsically-disordered proteins
- (2020) Chih-Yung S Lee et al. eLife
- Competing Protein-RNA Interaction Networks Control Multiphase Intracellular Organization
- (2020) David W. Sanders et al. CELL
- G3BP1 Is a Tunable Switch that Triggers Phase Separation to Assemble Stress Granules
- (2020) Peiguo Yang et al. CELL
- RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation
- (2020) Jordina Guillén-Boixet et al. CELL
- The Wide World of Coacervates: From the Sea to Neurodegeneration
- (2020) Emanuele Astoricchio et al. TRENDS IN BIOCHEMICAL SCIENCES
- Mechanisms and Regulation of RNA Condensation in RNP Granule Formation
- (2020) Devin Tauber et al. TRENDS IN BIOCHEMICAL SCIENCES
- Intrinsically Disordered Regions Direct Transcription Factor In Vivo Binding Specificity
- (2020) Sagie Brodsky et al. MOLECULAR CELL
- RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43
- (2019) Jacob R. Mann et al. NEURON
- Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report
- (2019) Peter T Nelson et al. BRAIN
- Cross-Regulation between TDP-43 and Paraspeckles Promotes Pluripotency-Differentiation Transition
- (2019) Miha Modic et al. MOLECULAR CELL
- TDP-43 proteinopathy and mitochondrial abnormalities in neurodegeneration
- (2019) Ju Gao et al. MOLECULAR AND CELLULAR NEUROSCIENCE
- Alternative Splicing Regulatory Networks: Functions, Mechanisms, and Evolution
- (2019) Jernej Ule et al. MOLECULAR CELL
- Phase separation-deficient TDP43 remains functional in splicing
- (2019) Hermann Broder Schmidt et al. Nature Communications
- The SINEB1 element in the long non-coding RNA Malat1 is necessary for TDP-43 proteostasis
- (2019) Tuan M Nguyen et al. NUCLEIC ACIDS RESEARCH
- Physical Principles and Extant Biology Reveal Roles for RNA-Containing Membraneless Compartments in Origins of Life Chemistry
- (2018) Raghav R. Poudyal et al. BIOCHEMISTRY
- The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43
- (2018) Hao-Ru Li et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains
- (2018) Lin Guo et al. CELL
- A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing
- (2018) Ailin Wang et al. EMBO JOURNAL
- Novel genes associated with amyotrophic lateral sclerosis: diagnostic and clinical implications
- (2018) Ruth Chia et al. LANCET NEUROLOGY
- Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation
- (2018) Veronica H. Ryan et al. MOLECULAR CELL
- Functional Domains of NEAT1 Architectural lncRNA Induce Paraspeckle Assembly through Phase Separation
- (2018) Tomohiro Yamazaki et al. MOLECULAR CELL
- TDP-43 gains function due to perturbed autoregulation in a Tardbp knock-in mouse model of ALS-FTD
- (2018) Matthew A. White et al. NATURE NEUROSCIENCE
- RNA buffers the phase separation behavior of prion-like RNA binding proteins
- (2018) Shovamayee Maharana et al. SCIENCE
- mRNA structure determines specificity of a polyQ-driven phase separation
- (2018) Erin M. Langdon et al. SCIENCE
- Heteromeric RNP Assembly at LINEs Controls Lineage-Specific RNA Processing
- (2018) Jan Attig et al. CELL
- Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization
- (2018) Leeanne McGurk et al. MOLECULAR CELL
- Compartmentalised RNA catalysis in membrane-free coacervate protocells
- (2018) Björn Drobot et al. Nature Communications
- RNA phase transitions in repeat expansion disorders
- (2017) Ankur Jain et al. NATURE
- Thiol-linked alkylation of RNA to assess expression dynamics
- (2017) Veronika A Herzog et al. NATURE METHODS
- Salmon provides fast and bias-aware quantification of transcript expression
- (2017) Rob Patro et al. NATURE METHODS
- High-Resolution RNA Maps Suggest Common Principles of Splicing and Polyadenylation Regulation by TDP-43
- (2017) Gregor Rot et al. Cell Reports
- Liquid–liquid phase separation in cellular signaling systems
- (2016) P Andrew Chong et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- irCLIP platform for efficient characterization of protein–RNA interactions
- (2016) Brian J Zarnegar et al. NATURE METHODS
- ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain
- (2016) Alexander E. Conicella et al. STRUCTURE
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
- (2015) Avinash Patel et al. CELL
- hiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1
- (2015) Yoichiro Sugimoto et al. NATURE
- TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
- (2015) J. P. Ling et al. SCIENCE
- Gem Depletion: Amyotrophic Lateral Sclerosis and Spinal Muscular Atrophy Crossover
- (2014) Ruben J. Cauchi CNS Neuroscience & Therapeutics
- Targeting TDP-43 in neurodegenerative diseases
- (2014) Mauricio Budini et al. EXPERT OPINION ON THERAPEUTIC TARGETS
- Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
- (2013) Hong Joo Kim et al. NATURE
- Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
- (2013) Peter J Lukavsky et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- STAR: ultrafast universal RNA-seq aligner
- (2012) Alexander Dobin et al. BIOINFORMATICS
- Phase transitions in the assembly of multivalent signalling proteins
- (2012) Pilong Li et al. NATURE
- Integrative Genome-wide Analysis Reveals Cooperative Regulation of Alternative Splicing by hnRNP Proteins
- (2012) Stephanie C. Huelga et al. Cell Reports
- Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
- (2011) Magdalini Polymenidou et al. NATURE NEUROSCIENCE
- Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
- (2011) James R Tollervey et al. NATURE NEUROSCIENCE
- Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration
- (2010) Agnes L. Nishimura et al. BRAIN
- TDP-43 regulates its mRNA levels through a negative feedback loop
- (2010) Youhna M Ayala et al. EMBO JOURNAL
- iCLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution
- (2010) Julian König et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
- (2010) S.-C. Ling et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Identification of casein kinase-1 phosphorylation sites on TDP-43
- (2009) Fuyuki Kametani et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins
- (2009) Simon Alberti et al. CELL
- TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity
- (2009) Brian S. Johnson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis
- (2008) J. Sreedharan et al. SCIENCE
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExploreDiscover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversation