| Literature DB >> 21281565 |
Justin A Ross1, Michelle A Digman2, Lei Wang3, Enrico Gratton2, Joseph P Albanesi3, David M Jameson4.
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.Entities:
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Year: 2011 PMID: 21281565 PMCID: PMC3030261 DOI: 10.1016/j.bpj.2010.12.3703
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033