By Dr. Douglas R. Waverly, Professor Emeritus of Biochemistry, Yale University

Since lipid bilayers are self-assembled macroscopic aggregates, their constituent lipid molecules can spontaneously transition between the two leaflets. This so

Two of our recent findings on condensates were posted on bioRxiv! In the first one, Huan made a surprising discovery that the excitation of fluorescently tagged proteins leads to condensate-mediated …...

MINFLUX nanoscopy reveals subcellular distribution and conformational diversity of PIEZO1 channels in intact cells.

The cell nucleus is constantly subjected to forces under many fundamental biological processes, including confined cell migration, osmoregulation, and large-scale stresses across tissues during develo...

Membranes form the intricately shaped compartments of life. The Biomembrane Days are a triannual workshop that highlights recent advances in understanding the morphology and molecular organization of ...

In this Review, Lusk et al. discuss emerging insights into nuclear pore complex variability with regard to composition and dilation state, and propose nuclear mechanics as a key determinant of driving...

Beyond its known role in stabilizing microtubules, it is now shown that tau protein actively promotes lattice defect repair by enhancing tubulin turnover at topological defects.

Cornell researchers have uncovered the surprising role played by a “three-tailed” fat molecule in cellular survival during heart attack and stroke: protecting the cells against damage when oxygen runs...

Voltage-gated ion channels are found in many membrane-enclosed structures, including synaptic vesicles, endosomes, mitochondria, chloroplasts, viruses and bacteria. In small compartments, assumptions ...

Biomolecular condensates are protein-dense regions in cells that often arise from liquid–liquid phase separation. Interfacial tension is a key determinant of biomolecular condensate behavior, influencing condensate size and interactions with intracellular structures. Certain proteins and RNAs are known to selectively localize to the interface of condensates, where they can regulate condensate function in cells. Previously, we designed amphiphilic proteins that preferentially adsorb to the surface of condensates. These proteins contain one condensate-philic domain (RGG) and one condensate-phobic domain (MBP or GST). Here, we demonstrate through direct quantification that these amphiphilic proteins act as surfactants, reducing the interfacial tension of RGG–RGG condensates from ∼260 to ∼100 μN/m in a concentration-dependent manner. Notably, the GST-based surfactant protein exhibits a 10-fold greater efficacy in lowering interfacial tension compared with the MBP-based surfactant. We show that this increased efficacy is due to its higher surface density, driven by GST’s ability to oligomerize. We also show that these surfactant proteins slow droplet fusion and reduce the average droplet size, as would be expected of a typical surfactant. Our findings quantitatively show how surfactant proteins can play a critical role in regulating the behavior of biomolecular condensates by modulating their interfacial tension.

The SARS-CoV-2 Nucleocapsid (N) protein serves multiple roles in the viral lifecycle. Phosphorylation toggles N between these roles by altering N’s conformation, its material properties when phase sep...

Holly Cheng and her colleagues were the first to successfully use micropipette aspiration to measure parts from a living cell while they were still biologically active