In vitro reconstitution shows how HIV-1 Gag assemblies on membranes can package the RNA genome in the presence of a vast excess of competing cellular RNAs, and that selectivity and immature lattice assembly are deeply intertwined with one another.
Theoretical analysis and in vitro reconstitution of a biological reaction-diffusion system identify key functional motifs as well as underlying principles and enable rebuilding pattern formation in a modular fashion.
Purification of two conserved protein complexes, the γ-TuRC and Augmin, using a simple affinity technique, demonstrates that they are necessary and sufficient for the essential phenomenon of branching microtubule nucleation.
The geometry selection rules of dynamic Min protein patterns are determined in fully confined fluidic chambers, showing that both oscillations and running waves are derivatives of spiral rotations that are established as the majority pattern.
A reconstituted system has been developed that self-organizes into dynamic actin cortices capable of spontaneous polarization, similar to the initial cortical polarization observed in cells during embryogenesis and development.
A combination of cryo-electron microscopy of TPX2 bound to microtubules and in vitro reconstitution experiments reveals a novel microtubule interaction mode that explains how TPX2 promotes microtubule nucleation and stabilization.