How does FtsZ's treadmilling help bacterial cells divide?

Most bacteria assemble a ring-like macromolecular machinery scaffolded by the essential cytoskeletal protein FtsZ for cell division. Studies have broadly explored how FtsZ could polymerize at the correct place and time. Recently, the FtsZ-ring was found to exhibit dynamic treadmilling along the circumference of the division site, driven by GTP hydrolysis. This apparently directional motion of FtsZ seems to drive the movement of septal cell wall synthesis enzymes and to play an important role in modulating cell envelope constriction and septum morphogenesis. However, the relationship between FtsZ's treadmilling dynamics and cell wall synthesis varies in different bacteria. More importantly, the biophysical and molecular mechanisms governing these dynamic processes are unclear. In this viewpoint, we will focus on some new and exciting studies surrounding this topic and discuss potential mechanisms that underlie how FtsZ's treadmilling dynamics might regulate septal cell wall synthesis and cell division.