Garrotes, springs, ratchets, and whips: putting dynamin models to the test.
The GTPase dynamin is essential for clathrin-mediated endocytosis. Numerous new and exciting discoveries regarding dynamin function in vivo and in vitro have led to various models in which dynamin functions directly in membrane fission and the release of clathrin-coated vesicles from the plasma membrane. This would make dynamin unique among GTPases in its ability to act as a mechanochemical enzyme. Here we review the various models and their supporting data. We then discuss new findings that raise doubts as to whether dynamin breaks the paradigm that governs regulatory GTPases.
Sever
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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Dana Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA.
Damke
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Schmid
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D000818:Animals; D034281:Dynamins; D004548:Elasticity; D004705:Endocytosis / Q000502:physiology; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D008081:Liposomes; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D008081:Liposomes; D020409:Molecular Motor Proteins; D009419:Nerve Tissue Proteins; C075637:amphiphysin; D006160:Guanosine Triphosphate; D020558:GTP Phosphohydrolases; D034281:Dynamins