Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.[5][6]
Dynamin possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the dynamin, which can also self-assemble leading to stimulation of GTPase activity. More than sixty highly conserved copies of the 3' region of this gene are found elsewhere in the genome, particularly on chromosomes Y and 15. Alternatively spliced transcript variants encoding different isoforms have been described.[7]
De novo mutations in DNM1 have been associated with a severe form of childhood epilepsy called developmental and epileptic encephalopathy. Most pathogenic variants are missense variants, and have been shown to impair synaptic vesicle endocytosis in a dominant negative manner.[8]
DNM1 has been shown to interact with:
PDB gallery
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1dyn: CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN
2aka: Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin 1 from Rattus norvegicus
2dyn: DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)
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RME/Clathrin |
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