| Type: | Domain | Name: | GTPase effector domain, GED |
| Description: | Dynamin superfamily members are large GTPases, conserved through evolution, mainly described as mechanochemical enzymes involved in membrane scission events. The dynamin superfamily has been subdivided into several subgroups based on domain organisation: classical dynamin, dynamin-like proteins (Dlps), Mc proteins, optic atrophy 1 protein (OPA1), Mitofusins, guanylate-binding proteins (GBP) and alastatins. All members display a common architecture: a large GTPase (see ) domain followed by a 'middle domain' of ill-defined function and a downstream coiled-coil GTPase effector domain (GED) that functions in higher order assembly and as a GTPase activating protein (GAP) for dynamin's GTPase activity. Most members contain additional domains that characterise the different subgroups. For example, classical dynamins contain a lipid binding Pleckstrin-homology (PH) (see ) domain between the middle domain and the GED domain as well as a C-terminal proline-arginine rich domain (PRD) that interacts with numerous SH3 domain-containing binding partners while Dlps lack the PRD but have a PH domain, which may, however, be highly divergent. These various domains confer a variety of biochemical properties and cellular localisations to dynamin, that may explain the diversity of their biological implications in endocytosis, intracellular traffic, organelle fission and fusion, cytokinesis and pathogen resistance [, , , ].The GED is seen to be largely helical in nature, and its oligomerisation occurs via intermolecular packing of the helices []. | Short Name: | GTPase_effector_domain_GED |
