In the cytosol, the proteins constituting cell-matrix adhesion sites form multi-protein building blocks which enter and leave these sites unaltered, thereby contributing to their rapid and correct self-assembly.

A novel retinal ganglion cell requires a cell adhesion molecule to grow its dendrites, collect synaptic inputs, and become selective to edges placed in its receptive field.

Data-driven mathematical modeling suggests that leading neural crest cells in a moving stream can robustly communicate with trailing cells by remodeling their extracellular matrix, thereby enabling long-distance collective migration.

Controlling cell cycle progression in a developing embryo directly depends on de novo histone supply and a specialized surveillance mechanism for nucleosome assembly.

CPEB4's switch from translational repressor to activator is regulated during cell cycle by hyperphosphorylation of its intrinsically disordered domain, which controls its phase-separation into RNA-containing liquid-like droplets.

Contractility wins over the polarity pathway in a tug-of-war to position a cytokinesis-like actomyosin ring at the equator of notochord cells.

Kidney organoids are a high-fidelity system for investigating basement membrane regulation in development and disease.

Ribosome assembly is monitored to promote proteostatis through a system whereby unassembled ribosomal proteins lead to activation of heat shock factor 1 and inactivation of the RP gene activator Ifh1.

Investigations of binding of the scaffold protein PICK1 to transmembrane proteins in their native membrane environment demonstrate potent but slow dynamics and reveal distinct binding modes supporting different biological functions.

Analysis of protein interfaces suggests cotranslational assembly can be an adaptive process, likely serving to minimise non-specific interactions with other proteins in the cell.