ArticleScientific reports2021
Shared and divergent phase separation and aggregation properties of brain-expressed ubiquilins.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 28 citations in OpenAlex.
- ALS mutations disrupt self-association between the ubiquilin STI1 hydrophobic groove and internal placeholder sequences.The EMBO journal · 2026Article
- STI1 domain engages transient helices to mediate Dsk2 phase separation and proteasome condensation.The EMBO journal · 2026Article
- Comparative proteomic analysis of Porphyromonas gingivalis challenged human dental pulp stem cells.Scientific reports · 2025Article
- Ubiquilin-2 liquid droplets catalyze α-synuclein fibril formation.The EMBO journal · 2025Article
- Short disordered termini and proline-rich domain are major regulators of UBQLN1/2/4 phase separation.Biophysical journal · 2024Article
- Pathogenic mutations in UBQLN2 exhibit diverse aggregation propensity and neurotoxicity.Scientific reports · 2024Article
- Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.Cellular and molecular life sciences : CMLS · 2023Article
- E6AP AZUL interaction with UBQLN1/2 in cells, condensates, and an AlphaFold-NMR integrated structure.Structure (London, England : 1993) · 2023Article
- UBQLN2 undergoes a reversible temperature-induced conformational switch that regulates binding with HSPA1B: ALS/FTD mutations cripple the switch but do not destroy HSPA1B binding.Biochimica et biophysica acta. General subjects · 2023Article
- Ubiquilin-2 regulates pathological alpha-synuclein.Scientific reports · 2023Article
- Mechanistic insights into enhancement or inhibition of phase separation by different polyubiquitin chains.EMBO reports · 2022Article
- 14-3-3 Proteins are Potential Regulators of Liquid-Liquid Phase Separation.Cell biochemistry and biophysics · 2022Review
- Protein lifetimes in aged brains reveal a proteostatic adaptation linking physiological aging to neurodegeneration.Science advances · 2022Article
- RTL8 promotes nuclear localization of UBQLN2 to subnuclear compartments associated with protein quality control.Cellular and molecular life sciences : CMLS · 2022Article
- Disrupting the Balance of Protein Quality Control Protein UBQLN2 Accelerates Tau Proteinopathy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
The brain-expressed ubiquilins, UBQLNs 1, 2 and 4, are highly homologous proteins that participate in multiple aspects of protein homeostasis and are implicated in neurodegenerative diseases. Studies have established that UBQLN2 forms liquid-like condensates and accumulates in pathogenic aggregates, much like other proteins linked to neurodegenerative diseases. However, the relative condensate and aggregate formation of the three brain-expressed ubiquilins is unknown. Here we report that the three ubiquilins differ in aggregation propensity, revealed by in-vitro experiments, cellular models, and analysis of human brain tissue. UBQLN4 displays heightened aggregation propensity over the other ubiquilins and, like amyloids, UBQLN4 forms ThioflavinT-positive fibrils in vitro. Measuring fluorescence recovery after photobleaching (FRAP) of puncta in cells, we report that all three ubiquilins undergo liquid-liquid phase transition. UBQLN2 and 4 exhibit slower recovery than UBQLN1, suggesting the condensates formed by these brain-expressed ubiquilins have different compositions and undergo distinct internal rearrangements. We conclude that while all brain-expressed ubiquilins exhibit self-association behavior manifesting as condensates, they follow distinct courses of phase-separation and aggregation. We suggest that this variability among ubiquilins along the continuum from liquid-like to solid informs both the normal ubiquitin-linked functions of ubiquilins and their accumulation and potential contribution to toxicity in neurodegenerative diseases.
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