Dynamin is a GTPase involved in membrane remodeling, particularly in endocytic membrane fission. It plays a critical role in endocytosis, with its function studied using various approaches including live cell imaging, cell-free studies, X-ray crystallography, and genetic studies in mice. Dynamin has three isoforms in mammals: Dynamin 1, 2, and 3, each with distinct expression patterns and functions. Dynamin 1 is mainly expressed in neurons, Dynamin 2 is ubiquitously expressed, and Dynamin 3 is found in the brain and testis. Dynamin-like proteins (DLPs) are a family of GTPases involved in membrane remodeling, with similar catalytic mechanisms to dynamin. The GTPase domain of dynamin undergoes dimerization and GTP hydrolysis, which is crucial for its function. Dynamin's domain organization includes a G domain, a middle region, a PH domain, a GED domain, and a proline-rich C-terminal region. Dynamin interacts with various proteins, including SH3 domain-containing proteins, to localize at endocytic sites and coordinate its function. Dynamin polymerizes into rings and helices, which are essential for membrane fission. Dynamin is involved in clathrin-mediated endocytosis, and its function is essential for synaptic vesicle recycling. Dynamin also plays a role in cytokinesis and the nervous system, with Dynamin 1 and 3 being particularly important for synaptic function. Dynamin mutations have been linked to various diseases, including Charcot-Marie-Tooth disease and centronuclear myopathy. Dynamin 1 has also been implicated in epilepsy, with mutations affecting its function and leading to neurological symptoms. Dynamin's role in membrane fission and its interactions with other proteins are areas of ongoing research.Dynamin is a GTPase involved in membrane remodeling, particularly in endocytic membrane fission. It plays a critical role in endocytosis, with its function studied using various approaches including live cell imaging, cell-free studies, X-ray crystallography, and genetic studies in mice. Dynamin has three isoforms in mammals: Dynamin 1, 2, and 3, each with distinct expression patterns and functions. Dynamin 1 is mainly expressed in neurons, Dynamin 2 is ubiquitously expressed, and Dynamin 3 is found in the brain and testis. Dynamin-like proteins (DLPs) are a family of GTPases involved in membrane remodeling, with similar catalytic mechanisms to dynamin. The GTPase domain of dynamin undergoes dimerization and GTP hydrolysis, which is crucial for its function. Dynamin's domain organization includes a G domain, a middle region, a PH domain, a GED domain, and a proline-rich C-terminal region. Dynamin interacts with various proteins, including SH3 domain-containing proteins, to localize at endocytic sites and coordinate its function. Dynamin polymerizes into rings and helices, which are essential for membrane fission. Dynamin is involved in clathrin-mediated endocytosis, and its function is essential for synaptic vesicle recycling. Dynamin also plays a role in cytokinesis and the nervous system, with Dynamin 1 and 3 being particularly important for synaptic function. Dynamin mutations have been linked to various diseases, including Charcot-Marie-Tooth disease and centronuclear myopathy. Dynamin 1 has also been implicated in epilepsy, with mutations affecting its function and leading to neurological symptoms. Dynamin's role in membrane fission and its interactions with other proteins are areas of ongoing research.