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Posts tagged #LLPs

Congrats to the authors on a beautiful study! 🥳 Very elegant dissection of #LLPS by Rubisco inside the pyrenoid. Our Ape1’s linker is N-terminal, here it’s a separate protein—yet the physics feels strikingly similar. Cryo-ET of disordered networks is tough, but that’s why this work is so impressive.

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Happy to share our deep characterization of #LLPS events modulating the DNA damage response (#DDR) through #53BP1 condensation promoted by #dincRNA
www.biorxiv.org/content/10.6...

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You like #LLPS? #TeamTomo? #Rubisco? Check out our latest preprint!

What a great collaboration this has been!

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Phase-separating fusion proteins drive cancer by upsetting transcription regulation - Genome Biology Background Numerous cellular processes rely on biomolecular condensates formed through liquid–liquid phase separation (LLPS). Recently, it has become evident that somatic mutations can interfere with ...

Catching up after not being too active recently:
In one of our most #interdisciplinary #multimodal research articles published last year, we demonstrated that #LLPS #condensate dysregulation is very widespread in somatic #cancer. We also provided mechanistic explanations for #oncofusion #proteins.

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Really valuable #preprint on biological #condensates, with some welcome terminological clarity:“Some papers equate condensates with #LLPS, but it is often neither clear whether the involved objects have liquid-like properties…nor whether they actually form by phase separation.”👏👇

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Captured a very obvious phase separation and fusion process (nuclear localization of tobacco cells)
#LLPS #phaseseparation

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Phase Behavior of TDP-43 and hnRNP H1: From Soluble and Aggregated States to Liquid-Like Droplets Cytotoxic inclusions of TAR DNA-binding protein 43 (TDP-43) have been identified in various neurodegenerative diseases. Mediated by its low-complexity C-terminal domain (CTD), TDP-43 can undergo liqui...

Updated pre-print published on TDP-43 phase transition controlled by effective method, #LLPS, #LCD, #hnRNP
www.biorxiv.org/content/10.1...

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Arthur Wong comments on s80 of Finance Act 2025, limited liability partnerships, in Finance Act edition of @thomsonreutersnews.bsky.social's British Tax Review, exploring the scope – and limitations – of this new legislation.

Read his article here: tinyurl.com/3w55r93n

#llps #s80FinanceAct2025

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🫣

#LLPS #Droplets #phaseseparation

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Don't forget to sign up for webinar on 27 Nov which Ten Old Square + @pumptax.bsky.social are giving on the major changes to the taxation of LLPs anticipated from Autumn Budget 2025.

Details here: tinyurl.com/3wxrrts7

#November2025budget #Autumn2025budget #LLPs

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Targeting the Liquid–Liquid Separation Region of c‐Maf for Treating Chromosomal Translocations in Multiple Myeloma Targeting the liquid-liquid separation region of c-Maf for treating pathogenic chromosomal translocations in multiple myeloma. c-Maf promotes cell proliferation by forming liquid–liquid phase separat....

#Article in #MedComm
Targeting the Liquid–Liquid Separation Region of c-Maf for Treating Chromosomal Translocations in Multiple Myeloma doi.org/10.1002/mco2...

#BenzoylBenzoicAcid #cMaf #ChromosomalTranslocation #LLPS #MultipleMyeloma #IDRs #BBA

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Many thanks #AntonioCostaFilho for the kind invitation to participate in the pre-meeting #SBBf course “Phase separation at membrane interphases: Biomolecular condensates in Actions”. Happy share session with #RumianaDimova #Condensates #LLPS #Bioimaging #Phasors #DANprobes

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Non-equilibrium demixing and dissolution of chiral coacervates via intrinsic catalysis Nature Communications - Constructing synthetic mimics of membraneless organelles using small molecules can contribute towards our understanding of active phase separation and their role in the...

Lighting up this Diwali, just out @natcomms.nature.com non-equilibrium demixing & dissolution of chiral coacervates via intrinsic catalysis rdcu.be/eL8mo
#SystemsChemistry, #NonEquilibrium, #LifeLikeSystems, #LLPS
Grateful @IISERKolkata, @ANRF_India Swarnajayanti Award @DBTIndia

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Computational investigation of the sequence context of arginine/glycine-rich motifs in the human proteome - BMC Genomics Arginine-glycine (RG)-rich motifs are among the most prevalent RNA-binding elements within intrinsically disordered regions (IDRs) of proteins and play crucial roles in RNA metabolism, gene regulation, and the formation of membraneless organelles via liquid phase separation (LLPS). Despite their biological relevance and implication in neurological disorders and cancer, the sequence features and context dependencies that define functional RG motifs remain poorly characterized owing to their disordered nature and sequence variability. In this study, we present a computational framework to dissect the sequence and structural context of RG motifs across the human proteome. By contrasting a functionally defined positive dataset—enriched for RNA-binding and phase-separating proteins—with a negative dataset of RG motif proteins lacking these annotations, we identified distinct compositional and contextual signatures. RG motifs in the functionally defined positive dataset show increased enrichment of phenylalanine, tyrosine, aspartic acid, and asparagine, both within and around the motif, as well as nonrandom spatial relationships with structured RNA-binding domains. Notably, phenylalanine and tyrosine exhibit divergent positional and functional profiles, suggesting distinct mechanistic roles. Our analysis highlights the potential of sequence-based approaches to uncover functional determinants in disordered protein regions and further advances our understanding of the properties of RG motifs, offering a transferable framework for the study of other low-complexity motifs.

🖥️ New Publication Alert
Congratulations to Eric Schumbera, @dormannlab.bsky.social, @waltherlab.bsky.social & @miguelandrade66.bsky.social on their recent publication in BMC Genomics
#RGmotifs #IDRs #LLPS #HumanProteome #ComputationalMotifAnalysis
bmcgenomics.biomedcentral.com/articles/10....

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ha ha, according to clarivate, it could be #LLPS for #chemnobel 😁

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🧬 📰 In a News & Views article published in @nataging.nature.com, Prof. Nektarios Tavernarakis discusses the discovery of specialized mRNA translation hubs that form by #LLPS on the surface of #mitochondria to supply key proteins on-site, thus, upholding mitochondrial integrity and function.

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Constructing synthetic nuclear architectures via transcriptional condensates in a DNA protonucleus - Nature Communications Nuclear biomolecular condensates are functional sub-compartments within the cell nucleus. Here, the authors develop a synthetic DNA protonucleus that enables RNA transcription and condensation into di...

🚨Miao's and Weixiang's work on RNA transcription in DNA based condensates as nucleus mimics is now out in @natcomms.nature.com www.nature.com/articles/s41...
#syncell #DNA #condensate #LLPS.
Great work to understand transcription and LLPS in #crowded #viscoelastic environments @sfb1551.bsky.social

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Promiscuous and multivalent interactions between Eps15 and partner protein Dab2 generate a complex interaction network - Nature Communications Eps15, a protein involved in endocytosis initiation, uses small folded EH domains to bind disordered partner proteins and its own disordered tail, thus forming a dynamic network via phase separation t...

I am happy to share our new article on dynamic Eps15 and Dab2 networks in endocytosis studied by #NMR, and forming #LLPS. Research was done at @fmp-berlin.de and at the Institut de Biologie Structurale (IBS).

www.nature.com/articles/s41...

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The Role of Protein Aggregation in Neural Cell Differentiation Revealed by ATRX Phase Separation Recent research uncovers how ATRX protein aggregation influences neural cell differentiation, providing insights into developmental disorders and new treatment avenues.

The Role of Protein Aggregation in Neural Cell Differentiation Revealed by ATRX Phase Separation #Japan #Tokyo #ATRX #neural_stem_cells #LLPS

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💊 Small molecules that regulate phase separation may hold the key to treating cancer, neurodegeneration, and more. A recent review published in The FASEB Journal explores their mechanisms and drug discovery potential.
🔗 buff.ly/1hrR8Pv
#DrugDiscovery #LLPS #FASEBJournal

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You may have noticed the C2A and C2A-B linker domains are not resolved in the average. The reason we found in the linker sequence. They are intrinsically disordered regions (IDRs): glycine-rich, polyampholytic and predicted to be highly prone to phase-separate.

🧵10/n #LLPS

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Cells expressing Yap (stained green). Left side without  condensate induction, right side two minutes after condensate induction, now filled with green dots.

Cells expressing Yap (stained green). Left side without condensate induction, right side two minutes after condensate induction, now filled with green dots.

Please share …. 🙏
📣 Very soon, we’ll have an open PhD position starting in fall 2025 — this time not on cilia, but on YAP & TAZ in podocytes and their regulation via LLPS. Interested candidates are welcome to contact us directly.

Supervision by Inês Cabrita […]

[Original post on social.cologne]

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Endogenous retrovirus-like proteins recruit UBQLN2 to stress granules and shape their functional biology Virus-like proteins help our cells respond to environmental stress.

Our paper discovering novel roles for the retrovirus-like proteins RTL8 and PEG10 in shaping stress granule biology is now online on Science Advances! #llps #stressgranules

www.science.org/doi/full/10....

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Our new preprint 🧬🔗 www.biorxiv.org/content/10.1...
BRD4-NUT forms liquid-like condensates that locally constrain nucleosomes via BRD4-mediated crosslinking— physical control of #chromatin by #LLPS transcription condensates. @semeigazin.bsky.social @katsuminami.bsky.social @masaashimazoe.bsky.social

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Diagram of how intrinsically disordered proteins and phase-separated condensates coordinate presynaptic active zone structure and function. The presynaptic terminal organizes neurotransmission through dynamic and spatially structured protein assemblies. Synaptic vesicles (SVs) are distributed between a docked pool at the AZ and a reserve pool. Precise coupling between docked SVs and voltage-gated calcium channels enables rapid release, a process supported by an underlying AZ scaffold. Jin and colleagues propose that scaffold components, including Liprin-α and RIM, through their multifaceted intermolecular interaction, assemble into condensates via liquid-liquid phase separation (LLPS) that organize the molecular and functional architecture of the AZ. These dynamic assemblies help cluster SV release machinery while remaining responsive to synaptic activity. Thus, LLPS-driven Liprin-α/RIM condensates not only scaffold presynaptic architecture but also fine-tune vesicle priming and release dynamics. Created with BioRender.com.

Diagram of how intrinsically disordered proteins and phase-separated condensates coordinate presynaptic active zone structure and function. The presynaptic terminal organizes neurotransmission through dynamic and spatially structured protein assemblies. Synaptic vesicles (SVs) are distributed between a docked pool at the AZ and a reserve pool. Precise coupling between docked SVs and voltage-gated calcium channels enables rapid release, a process supported by an underlying AZ scaffold. Jin and colleagues propose that scaffold components, including Liprin-α and RIM, through their multifaceted intermolecular interaction, assemble into condensates via liquid-liquid phase separation (LLPS) that organize the molecular and functional architecture of the AZ. These dynamic assemblies help cluster SV release machinery while remaining responsive to synaptic activity. Thus, LLPS-driven Liprin-α/RIM condensates not only scaffold presynaptic architecture but also fine-tune vesicle priming and release dynamics. Created with BioRender.com.

Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @plosbiology.org study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease 🧪 Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

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Diagram of how intrinsically disordered proteins and phase-separated condensates coordinate presynaptic active zone structure and function. The presynaptic terminal organizes neurotransmission through dynamic and spatially structured protein assemblies. Synaptic vesicles (SVs) are distributed between a docked pool at the AZ and a reserve pool. Precise coupling between docked SVs and voltage-gated calcium channels enables rapid release, a process supported by an underlying AZ scaffold. Jin and colleagues propose that scaffold components, including Liprin-α and RIM, through their multifaceted intermolecular interaction, assemble into condensates via liquid-liquid phase separation (LLPS) that organize the molecular and functional architecture of the AZ. These dynamic assemblies help cluster SV release machinery while remaining responsive to synaptic activity. Thus, LLPS-driven Liprin-α/RIM condensates not only scaffold presynaptic architecture but also fine-tune vesicle priming and release dynamics. Created with BioRender.com.

Diagram of how intrinsically disordered proteins and phase-separated condensates coordinate presynaptic active zone structure and function. The presynaptic terminal organizes neurotransmission through dynamic and spatially structured protein assemblies. Synaptic vesicles (SVs) are distributed between a docked pool at the AZ and a reserve pool. Precise coupling between docked SVs and voltage-gated calcium channels enables rapid release, a process supported by an underlying AZ scaffold. Jin and colleagues propose that scaffold components, including Liprin-α and RIM, through their multifaceted intermolecular interaction, assemble into condensates via liquid-liquid phase separation (LLPS) that organize the molecular and functional architecture of the AZ. These dynamic assemblies help cluster SV release machinery while remaining responsive to synaptic activity. Thus, LLPS-driven Liprin-α/RIM condensates not only scaffold presynaptic architecture but also fine-tune vesicle priming and release dynamics. Created with BioRender.com.

Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @plosbiology.org study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease 🧪 Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

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Diagram of how intrinsically disordered proteins and phase-separated condensates coordinate presynaptic active zone structure and function. The presynaptic terminal organizes neurotransmission through dynamic and spatially structured protein assemblies. Synaptic vesicles (SVs) are distributed between a docked pool at the AZ and a reserve pool. Precise coupling between docked SVs and voltage-gated calcium channels enables rapid release, a process supported by an underlying AZ scaffold. Jin and colleagues propose that scaffold components, including Liprin-α and RIM, through their multifaceted intermolecular interaction, assemble into condensates via liquid-liquid phase separation (LLPS) that organize the molecular and functional architecture of the AZ. These dynamic assemblies help cluster SV release machinery while remaining responsive to synaptic activity. Thus, LLPS-driven Liprin-α/RIM condensates not only scaffold presynaptic architecture but also fine-tune vesicle priming and release dynamics. Created with BioRender.com.

Diagram of how intrinsically disordered proteins and phase-separated condensates coordinate presynaptic active zone structure and function. The presynaptic terminal organizes neurotransmission through dynamic and spatially structured protein assemblies. Synaptic vesicles (SVs) are distributed between a docked pool at the AZ and a reserve pool. Precise coupling between docked SVs and voltage-gated calcium channels enables rapid release, a process supported by an underlying AZ scaffold. Jin and colleagues propose that scaffold components, including Liprin-α and RIM, through their multifaceted intermolecular interaction, assemble into condensates via liquid-liquid phase separation (LLPS) that organize the molecular and functional architecture of the AZ. These dynamic assemblies help cluster SV release machinery while remaining responsive to synaptic activity. Thus, LLPS-driven Liprin-α/RIM condensates not only scaffold presynaptic architecture but also fine-tune vesicle priming and release dynamics. Created with BioRender.com.

Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @plosbiology.org study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease 🧪 Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

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#NatureReviews #DrugDiscovery #ProteinDisorder #ProteinEnsembles #TranscriptionFactors #BiomolecularCondensates #LLPS #imods #IDP #IDPs #HTS #HCS #Biophysics #StructuralBiology #Bioinformatics #ComputationalModeling #MolecularDynamics @viblifesciences.bsky.social @vubrussel.bsky.social

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Development of #drugs that modulate #protein condensates is increasingly being seen as a route for #drugdevelopment.
Here, "protein condensate inhibitors" were developed to target cGAS benefitting from NanoTemper's Monolith X's in-solution binding affinity measurement to calculate their Kds
#llps

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Hen and egg problem! If you look carefully into biological condensate literature you can find such sharp fronts, which went unnoticed - now we can explain this - and the importance can now be considered in biology.
#softmatter #biomolecularcondensates #DNAnanotech #LLPS #phaseseparation

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