GTPaseDynamin

GTPaseDynamin is a member of the dynamin family of GTPases, which are proteins that hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). Dynamin is involved in the regulation of membrane trafficking and is essential for the formation of clathrin-coated vesicles, which are involved in endocytosis, a process by which cells internalize molecules from the extracellular environment. Dynamin forms a helical structure around the neck of the vesicle, which constricts and pinches off the vesicle from the plasma membrane. This process is regulated by the binding of GTP to dynamin, which induces a conformational change that allows the protein to interact with other proteins involved in vesicle formation. Once the vesicle is formed, the GTP is hydrolyzed to GDP, which causes dynamin to release its interaction partners and the vesicle to be transported to the interior of the cell. Dynamin is a highly conserved protein, with homologs found in all eukaryotic organisms, and mutations in dynamin genes have been linked to various diseases, including Alzheimer's disease and Charcot-Marie-Tooth disease.