ArticleRare diseases (Austin, Tex.)2013
Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly.
Article in Rare diseases (Austin, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 46 citations in OpenAlex.
- Nuclear-import receptors remodel the dilute phase to suppress phase transitions of RNA-binding proteins with prion-like domains.bioRxiv : the preprint server for biology · 2025Article
- Transient Poly(ADP-Ribose) Triggers FUS Condensation Hysteresis via a Prion-Like Mechanism.bioRxiv : the preprint server for biology · 2025Article
- Cross-Effects in Folding and Phase Transitions of hnRNP A1 and C9Orf72 RNA G4 In Vitro.Molecules (Basel, Switzerland) · 2024Article
- Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD.Molecular neurodegeneration · 2024Review
- Saccharomyces cerevisiae as a research tool for RNA-mediated human disease.Wiley interdisciplinary reviews. RNA · 2023Review
- G3BP1-dependent mechanism suppressing protein aggregation in Huntington's models and its demise upon stress granule assembly.Human molecular genetics · 2023Article
- Article
- Discovering molecular features of intrinsically disordered regions by using evolution for contrastive learning.PLoS computational biology · 2022Article
- Heterogeneous nuclear ribonucleoprotein A2/B1 as a novel biomarker in elderly patients for the prediction of postoperative neurocognitive dysfunction: A prospective nested case-control study.Frontiers in aging neuroscience · 2022Article
- Characterization of HNRNPA1 mutations defines diversity in pathogenic mechanisms and clinical presentation.JCI insight · 2021Article
- Amyotrophic Lateral Sclerosis: Molecular Mechanisms, Biomarkers, and Therapeutic Strategies.Antioxidants (Basel, Switzerland) · 2021Review
- Multiple ways to a dead end: diverse mechanisms by which ALS mutant genes induce cell death.Cell cycle (Georgetown, Tex.) · 2021Review
- Combating deleterious phase transitions in neurodegenerative disease.Biochimica et biophysica acta. Molecular cell research · 2021Review
- Multiple Sclerosis-Associated hnRNPA1 Mutations Alter hnRNPA1 Dynamics and Influence Stress Granule Formation.International journal of molecular sciences · 2021Article
- Stress granule subtypes: an emerging link to neurodegeneration.Cellular and molecular life sciences : CMLS · 2020Review
- Karyopherins and condensates.Current opinion in cell biology · 2020Review
- Alternative Splicing of ALS Genes: Misregulation and Potential Therapies.Cellular and molecular neurobiology · 2020Review
- Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization.Nature communications · 2019Article
- Therapeutic Dissolution of Aberrant Phases by Nuclear-Import Receptors.Trends in cell biology · 2019Review
- Limb girdle muscular dystrophy D3 HNRNPDL related in a Chinese family with distal muscle weakness caused by a mutation in the prion-like domain.Journal of neurology · 2019Article
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2 authors at 2 institutions in 1 country.
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Abstract
Approximately 1% of human proteins harbor a prion-like domain (PrLD) of similar low complexity sequence and amino acid composition to domains that drive prionogenesis of yeast proteins like Sup35. PrLDs are over-represented in human RNA-binding proteins and mediate phase transitions underpinning RNP granule assembly. This modality renders PrLDs prone to misfold into conformers that accrue in pathological inclusions that characterize various fatal neurodegenerative diseases. For example, TDP-43 and FUS form cytoplasmic inclusions in amyotrophic lateral sclerosis (ALS) and mutations in TDP-43 and FUS can cause ALS. Here, we review our recent discovery of discrete missense mutations that alter a conserved gatekeeper aspartate residue in the PrLDs of hnRNPA2/B1 and hnRNPA1 and cause multisystem proteinopathy and ALS. The missense mutations generate potent steric zippers in the PrLDs, which enhance a natural propensity to form self-templating fibrils, promote recruitment to stress granules and drive cytoplasmic inclusion formation. PrLDs occur in ~250 human proteins and could contribute directly to the etiology of various degenerative disorders.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.