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. 2011 Feb 2;100(3):L15-L17.
doi: 10.1016/j.bpj.2010.12.3703.

Oligomerization State of Dynamin 2 in Cell Membranes Using TIRF and Number and Brightness Analysis

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Free PMC article

Oligomerization State of Dynamin 2 in Cell Membranes Using TIRF and Number and Brightness Analysis

Justin A Ross et al. Biophys J. .
Free PMC article

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.

Figures

Figure 1
Figure 1
TIRF intensity image of Dnm2-EGFP.
Figure 2
Figure 2
(A) Brightness-versus-intensity plot showing the tetrameric region (green box) and higher-order oligomers (red box). Number (B) and brightness (C) map of Dnm2-EGFP within the cell.

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