PLOS BiologyJul 28, 2025
The type I regulatory subunit of #ProteinKinaseA undergoes #LiquidLiquidPhaseSeparation #LLPS to help compartmentalize cAMP. This study shows that this tunes Ca2+ & cAMP oscillations in pancreatic #BetaCells, controlling #insulin secretion & regulating proliferation @PLOSBiology https://plos.io/4o9onKQ
Bernhard SchermerJul 26, 2025

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 and me, embedded within PodoSigN!
Within this project, close collab. with Beate Vollenbröker‘s team.

#Podocyte #Trr422 #Fsgs #Nephrolab #PhdPosition #Biology #Genetics #LLPS #HippoSignaling #phd

@CECAD
@cilia

Amyloid Research labJun 26, 2025

Two new articles from our lab:

Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction https://pubs.acs.org/doi/10.1021/acschemneuro.5c00086

Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related α-Synuclein https://pubs.acs.org/doi/10.1021/acs.biomac.5c00130

#VU #ACS #amyloid #LLPS #science

PLOS BiologyJun 12, 2025
Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @PLOSBiology study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease. Paper: https://plos.io/3Tj5CX7 Primer: https://plos.io/3HTacJ9
CellBioNewsMar 8, 2025

#Cellular structure without a #membrane: Researcher discusses how #synapses use #liquids to create functional separations.

#LLPS #membrane-less_organelles #neurotransmission

https://phys.org/news/2025-03-cellular-membrane-discusses-synapses-liquids.html

Cellular structure without a membrane: Researcher discusses how synapses use liquids to create functional separations

The laboratory of Ege Kavalali, professor and chair of the Department of Pharmacology, published a paper in Nature Communications that determined that liquid-liquid phase separation plays a key role within the nanostructure of synapses, and that its disruption affects evoked but not spontaneous neurotransmission.

Phys.org
Show threadDan BoseAug 15, 2024
This allows condensate behaviour to respond to different inputs, such as lysine #acetylation in IDRs in other CBP domains. It can help to explain how #transcription factors binding to different regions of CBP differentially regulate CBP activity. #enhancers #generegulation #llps #chromatin #imaging #biochemistry #molecularbiology #CellBiology
Amyloid Research labJul 10, 2024

Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"

https://www.biorxiv.org/content/10.1101/2024.07.05.602219v1

#LLPS, #vilniusuniversity, #lifesciencescenter #Research

Amyloid Research labApr 22, 2024

Hello Mastodon,

Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.

#LLPS #Science #LifeSciencesCenter #VilniusUniversity

PLOS BiologyMar 8, 2024
Meta-analysis of postsynaptic proteomes reveals 97 poorly studied proteins; @TakeshiKaizuka @ToruTakumi &co find that FAM81A regulates condensation of #postsynaptic proteins via #LLPS to affect the size & function of #synapses #PLOSBiology https://plos.io/48KDPnO
FAM81A is a postsynaptic protein that regulates the condensation of postsynaptic proteins via liquid–liquid phase separation

Proteomic analyses of postsynaptic proteins have mostly overlooked those with poorly characterized functions, likely missing crucial contributors to synaptic biology. Through a meta-analysis the authors identify 97 postsynaptic proteins with poorly characterized function, and elucidate the role FAM81A, revealing that it regulates the condensation of postsynaptic proteins via liquid-liquid phase separation to affect the size and function of synapses.

PLOS BiologyMar 1, 2024
Nuclear localization of #TDP43 is crucial for its function during #RNAprocessing & #neurodegeneration. @AyalaLab1 &co show that #RNAbinding & macromolecular assembly, including via #LLPS, play a central role in TDP-43 nuclear retention #PLOSBiology https://plos.io/3v372fT
RNA-mediated ribonucleoprotein assembly controls TDP-43 nuclear retention

TDP-43 nuclear localization is crucial for its function during RNA processing and pathogenesis of neurodegenerative disorders. This manuscript demonstrates that RNA binding and macromolecular assembly, through multivalent interactions and liquid-liquid phase separation, play a central role in TDP-43 nuclear retention.