Dynamins and dynamin-related proteins (DRPs) constitute a large superfamily of GTPases throughout animal, plant, and bacteria and play essential roles in core cellular processes (Praefcke and McMahon, 2004). Plant specific dynamin-related subfamilies share essential functions with those in mammalian cell, e.g. clarthrin-mediated endocytosis and fission of mitochondria; yet they also play unique functional roles in plant cells (Hong et al., 2003; Chen et al., 2011; Xue et al., 2011) (Supplementary Figure S1). Key features of dynamin members, including large molecular size, high basal GTP hydrolysis, and self-assembly into filamentous helices, distinguish them from other classical signaling and regulatory GTPases (Praefcke and McMahon, 2004). Dynamins are known to play a dual-role in clathrin-mediated endocytosis, in which the basal activity is necessary for early endocytic events and an assembly-stimulated activity is required in later stages of membrane fission (Sever et al., 1999). A mechanochemical model was presented focusing on dynamin in triggering the vesicle scission stimulated by GTP hydrolysis. In such a model, two distinct mechanisms, i.e. ‘pinchase’ and ‘poppase’, were proposed based on GTP hydrolysis induced dynamin vesiculation on liposomes (Sweitzer and Hinshaw, 1998). Differences between the two possible mechanisms focus on tightening the vesicle neck by dynamin oligomer to ‘pinching off’ the vesicle or a length-wise extension of the dynamin super helix to ‘popping off’’ of the vesicle mechanochemically (Praefcke and McMahon, 2004).