Summary
Dynamin is a large multidomain GTPase that assembles into helical arrays around the necks of deeply invaginated clathrin-coated pits and catalyzes membrane fission during the final stages of endocytosis. Although it is well established that the function of dynamin in vivo depends on its oligomerization and its capacity for efficient GTP hydrolysis, the molecular mechanisms governing these activities have remained poorly defined. In recent years, there has been an explosion of structural data that has provided new insights into the architecture, organization and nucleotide-dependent conformational changes of the dynamin fission machine. Here, we review the key findings of these efforts and discuss the implications of each with regard to GTP hydrolysis, dynamin assembly and membrane fission.
Funding
The work of our laboratory was supported by the Intramural Program of the National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK). J.S.C. is supported by a Nancy Nossal Fellowship award from NIDDK. Deposited in PMC for release after 12 months.
