Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor

Significance Dynamin is a protein that is a central player in endocytosis, a process that mediates the entry of diverse particles into cells, from nutrients to viruses. Dynamin’s primary activity is to use guanosine triphosphate as fuel to constrict and cut membrane tubes. Key quantitative aspects of its function remain yet unclear. In this work, we determine the strength of an individual dynamin motor. Then, by building a detailed computational model resolving individual motors, we demonstrate that dynamin produces sufficient force to tightly constrict a membrane tube when most of its motors are simultaneously cooperating. Hence, we quantitatively validate the prevailing constriction-by-ratchet model for nature’s strongest torque-generating motor: the dynamin “nanomuscle.”