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Oligomerization state of dynamin 2 in cell membranes using TIRF and number and brightness analysis.

  • Author(s): Ross, Justin A
  • Digman, Michelle A
  • Wang, Lei
  • Gratton, Enrico
  • Albanesi, Joseph P
  • Jameson, David M
  • et al.
Abstract

Dynamin 2 is an ubiquitously expressed ∼100 kDa GTPase involved in receptor-mediated endocytosis, Golgi budding, and cytoskeletal reorganization. Dynamin molecules assemble around the necks of budding vesicles and constrict membranes in a GTP-dependent process, resulting in vesicle release. The oligomerization state of dynamin 2 in the membrane is still controversial. We investigated dynamin 2 within the plasma membrane of live cells using total internal reflection microscopy coupled with number and brightness analysis. Our results demonstrate that dynamin 2 is primarily tetrameric throughout the entire cell membrane, aside from punctate structures that may correspond to regions of membrane vesiculation.

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