page_title: Dynamin
section_title: Structure
hierarchical_section_title: Dynamin / Structure
caption_attribution_description: English: Hinshaw, J. “Dynamin overview: The Role of Dynamin in Membrane Fission”. National institute of diabetes &amp; digestive &amp; kidney diseases, Laboratory of cell biochemistry and biology. http://dynamin.niddk.nih.gov/.
context_page_description: Dynamin is a GTPase responsible for endocytosis in the eukaryotic cell. Dynamin is part of the "dynamin superfamily", which includes classical dynamins, dynamin-like proteins, Mx proteins, OPA, mitofusins, and GBPs. Members of the dynamin family are principally involved in the scission of newly formed vesicles from the membrane of one cellular compartment and their targeting to, and fusion with, another compartment, both at the cell surface as well as at the Golgi apparatus. Dynamin family members also play a role in many processes including division of organelles, cytokinesis and microbial pathogen resistance.
context_section_description: Dynamin itself is a 96 kDa enzyme, and was first isolated when researchers were attempting to isolate new microtubule-based motors from the bovine brain. Dynamin has been extensively studied in the context of clathrin-coated vesicle budding from the cell membrane. Beginning from the N-terminus, Dynamin consists of a GTPase domain connected to a helical stalk domain via a flexible neck region containing  a Bundle Signalling Element  and GTPase Effector Domain. At the opposite end of the stalk domain is a loop that links to a membrane-binding Pleckstrin homology domain.  The protein strand then loops back towards the GTPase domain and terminates with a Proline Rich Domain that binds to the Src Homology domains of many proteins.
caption: Dynamin assembled into helical polymers as visualized by negative stain electron microscopy.[5]
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