Dynamin is a large GTPase whose GTP hydrolysis activity is required for the scission of clathrin-coated vesicles from the plasma membrane (reviewed in Ferguson and De Camilli, 2012). Dynamin is recruited to the plasma membrane through protein-protein interactions with many components of the clathrin-coated pit including ITSNs, SNX9 and 18 and amphiphysin (Lundmark and Carlsson, 2003; Soulet et al, 2005; David et al, 1996; Owen et al, 1998; Shupliakov et al, 1997). Although dynamin is recruited at lower levels throughout formation of the clathrin-coated pit, the bulk of dynamin is recruited at late stages, after the incorporation of BAR domain-containing proteins and actin-polymerizing factors (Ferguson et al, 2009; Taylor et al, 2011; Taylor et al, 2012; Posor et al, 2013; Meineke et al, 2013; Aguet et al, 2013; reviewed in Daumke et al, 2014). Several BAR domain proteins have SH3 domains that bind the proline rich domain (PRD) of dynamin. These interactions regulate dynamin GTPsae activity and vesicle formation (Neuman and Schmid, 2013). To facilitate scission of a clathrin-coated pit from the plasma membrane, dynamin self assembles into helical oligomers, stimulating its GTPase activity and contributing to the membrane remodeling required to form the neck of the emerging vesicle (Sweitzer and Hinshaw 1998; Yoshida et al, 2004; Chappie et al, 2010; Faelber et al, 2011; Ford et al, 2011; reviewed in McMahon and Boucrot, 2011; Daumke et al, 2014).