PROSITE documentation PDOC51388

GED domain profile

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 organization: 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 <PDOC00362>) 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 characterize the different subgroups. For example, classical dynamins contain a lipid binding Pleckstrin-homology (PH) (see <PDOC50003>) 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, by highly divergent. These various domains confer to dynamin a variety of biochemical properties and cellular localizations, that may explain the diversity of their biological implications in endocytosis, intracellular traffic, organelle fission and fusion, cytokinesis and pathogen resistance [1,2,3,4].

The GED is seen to be largely helical in nature, and its oligomerization occurs via intermolecular packing of the helices [2].

The profile we developed covers the entire GED domain.