The protein TPX2 and the protein complex augmin together recruit the microtubule nucleator γ-TuRC to a pre-existing microtubule where they initiate branching microtubule nucleation.

Biochemical and cell biological analyses reveal that the Astrin-SKAP complex acts to stabilize kinetochore-microtubule interactions through its intrinsic microtubule binding activity and its association with the Ndc80 complex, the core component of the kinetochore-microtubule interface.

DNA gyrase, a regulator of bacterial genomes topology, is shown to undergo rearrangements while functioning on DNA in vitro, with important potential consequences for gyrase-targeted antibiotics activity and bacterial evolution.

Compositional changes alter actin binding by phase separated T cell signaling clusters, enabling cluster movement by distinct actin networks.

The first reconstitution of an unconventional secretory mechanism uncovered the molecular mechanism by which Fibroblast Growth Factor 2 is secreted from mammalian cells.

Autophagic cargo receptors recruit the E3-like enzyme for Atg8 lipid conjugation to the cargo and thereby promote local formation of Atg8-positive autophagosomal membranes.

A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.

A systems level reconstitution of H-Ras GTPase signaling reveals a rich space of tunable dynamic outputs and clarifies the consequences of oncogenic perturbations to signaling.

Biophysical and structural studies reveal how low piconewton forces across actin enhance binding by the critical cell-cell adhesion protein α-catenin versus its force insensitive homolog vinculin.

A minimal cell-like system with defined geometry has been used to investigate the establishment and spatial control of a protein gradient that positions the bacterial cell division machinery.