Dynamin-related protein 1 (Drp1), the master regulator of mitochondrial division (MD), interacts with the cytoskeletal elements, namely filamentous actin (F-actin), microtubules (MT), and septins that coincidentally converge at MD sites. However, the mechanistic contributions of these critical elements to, and their cooperativity in, MD remain poorly characterized. Emergent data indicate that the cytoskeleton plays combinatorial modulator, mediator, and effector roles in MD by 'priming' and 'channeling' Drp1 for mechanoenzymatic membrane remodeling. In this brief review, we will outline our current understanding of Drp1-cytoskeleton interactions, focusing on recent progress in the field and a plausible 'diffusion barrier' role for the cytoskeleton in MD.