Structural and functional approaches unambiguously revealed physiologically relevant lateral interactions between FtsZ protofilaments.

The prokaryotic actin homologue MreB forms antiparallel double filaments in vitro and in vivo, an architecture that is unprecedented among the actin family of proteins.

Identification of a novel regulator that directly influences the assembly and function of the cell division machinery in industrially and medically important bacteria.

In budding yeast cells, slow monomeric septin GTPase activity and the cytosolic GTP:GDP ratio dictate the relative incorporation of alternative subunits during septin hetero-oligomer assembly, which proceeds by discrete, ordered steps dependent on allostery between interaction interfaces.

Snf7 crystal structures reveal the mechanisms of ESCRT-III activation and polymerization into membrane-remodeling filaments.

GpsB in Staphylococcus aureus directly regulates the central cell division protein FtsZ, a different function from that assigned for GpsB in other closely related organisms.

The architecture of the bacterial cytokinetic ring in cells and in artificial liposome reconstitutions has been described using electron microscopy, leading to a mechanism of constriction.

During sporulation, FtsAZ filaments mediating cell division in Bacillus subtilis are positioned asymmetrically around the septum only on the mother cell side, making the septum thinner than during vegetative growth.

A bacteriophage tubulin homolog, PhuZ, forms a structure with the biochemical, structural, and functional properties of a simplified, bipolar spindle.