Vesicle scission: dynamin.
Dynamin is a large GTPase involved in endocytic vesicle formation, but its exact role and mechanism are subjects of long-standing debate. Despite recent advances in the structural analyses of isolated dynamin domains and the faithful reconstitution of dynamin-dependent membrane fission in model membrane systems, the mechanism of its action remains poorly understood at the molecular level. Here, I will review current progress in elucidating dynamin action in vesicle scission and highlight the most visible gaps in knowledge that limit the development of a coherent and complete model for its role in vesicle biogenesis. Coordinated functions of BAR domain-containing binding partners are also discussed.
Ramachandran
Rajesh
R
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA. rxr275@case.edu
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D034281:Dynamins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009711:Nucleotides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D022161:Transport Vesicles / Q000378:metabolism*
D009711:Nucleotides; D034281:Dynamins