Cellular and structural insights into dynamin function during endocytic vesicle formation A tale of 50 years of investigation
Abstract: Dynamin is one of the major proteins involved in endocytosis. First identified 50 years ago in a genetic screen in Drosophila melanogaster, it has become a central player in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis, as well as other important cellular processes such as actin remodelling. Decades of work using biochemical and structural studies, cell-free assays, live cell imaging, acute inhibition and genetic studies have led to important insights on its mode of action. Dynamin is a remarkable mechano-GTPase which can do a lot to membranes on its own but which is, in cells, at the centre of a vast protein and lipid network and cannot work in isolation. These results have been synthetized in several important reviews and viewpoints [1–3]. In this review, I will summarize the main features of dynamin structure and function and its central role in membrane remodelling events, and give an update on the latest results.
Keywords: endocytosis / clathrin / dynamin / live cell imaging
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