Justin R. Houser

TL;DR: It is reported that intrinsically disordered domains of the endocytic adaptor proteins, Epsin1 and AP180 are highly potent drivers of membrane curvature, and a balance of steric pressure on the two surfaces of the membrane drives this exclusion.

TL;DR: It is demonstrated that steric exclusion within the crowded membrane environment can fundamentally limit the diffusive rate of proteins, regardless of their size, and this "speed limit" could be modulated by changes in local membrane coverage, providing a mechanism for tuning the rate of molecular interaction and assembly.

TL;DR: A sensor based on Förster resonance energy transfer (FRET) makes it possible to measure steric pressure in situ during diverse biochemical events that occur on membrane surfaces, such as membrane remodeling, ligand-receptor binding, assembly of protein complexes, and changes in membrane organization.

TL;DR: The results demonstrate that the impact of receptor heterodimerization on endocytic recruitment is controlled by a delicate balance between collaborative and competitive mechanisms.

TL;DR: Melcher et al. as discussed by the authors examined the states straddling the phase transition in terms of micro and macroscale properties, including mesh size, bundle diameter, persistence length, and intra-bundle spacing between filaments across the line of criticality.