Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, Hawaii.
Laboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, California.
Biophys J. 2011 Feb 2;100(3):L15-L17. doi: 10.1016/j.bpj.2010.12.3703.
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.
动力蛋白 2 是一种普遍表达的~100 kDa GTPase,参与受体介导的内吞作用、高尔基体出芽和细胞骨架重组。动力蛋白分子在出芽囊泡的颈部组装,并在 GTP 依赖性过程中收缩膜,导致囊泡释放。动力蛋白 2 在膜中的寡聚状态仍存在争议。我们使用全内反射显微镜结合数量和亮度分析研究了活细胞中的动力蛋白 2。我们的结果表明,动力蛋白 2 主要是四聚体,遍布整个细胞膜,除了点状结构,这些结构可能对应于膜出芽的区域。