Membrane Topography-Driven Movement of Biomolecular Condensates
Poellmann, M.; Zieske, K.
Show abstract
Biomolecular condensates are assemblies of proteins or nucleic acids that exhibit liquid-like properties and organize intracellular biochemical reactions within many cells. Some condensates require membrane association, and we previously developed an assay to reconstitute biomolecular condensates in the presence of different membrane topographies. However, the effect of membrane topography on the displacement of biomolecular condensates remains incompletely understood. Here, we studied the movement of biomolecular condensates on lipid membrane-clad microstructures in a cell-free assay. We observed upward movements within microgrooves for untethered condensates. Increased membrane attachment reduced the number of upward movements. Further increasing the membrane attachment led to the formation of elongated condensates. We demonstrated a coordinated sideward movement of these elongated condensates. Finally, we found that molecular crowding with Ficoll70 decreased the frequency of upward movements by slowing condensate growth. Our results indicate that membrane topographies, in combination with membrane attachment patterns, regulate passive biomolecular condensate movement.
Matching journals
The top 7 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Multivalent Interactions between Molecular Components Involved in Fast Endophilin Mediated Endocytosis Drive Protein Phase Separation 96%
- Remodeling of lipid-foam prototissues by network-wide tension fluctuations induced by active particles 96%
- Lipid packing and cholesterol content regulate membrane wetting and remodeling by biomolecular condensates. 96%
Similar papers in this journal
Similar papers in this journal
- Characterizing and controlling nanoscale self-assembly of suckerin-12 93%
- Light-inducible generation of membrane curvature in live cells with engineered BAR domain proteins 93%
- The Functional Nanopore Screen: A Versatile High-throughput Assay to Study and Engineer Protein Nanopores in Escherichia coli 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.