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

Justin A. Ross, Michelle A. Digman, Lei Wang, Enrico Gratton, Joseph P. Albanesi, David M. Jameson

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)L15-L17
JournalBiophysical journal
Volume100
Issue number3
DOIs
StatePublished - Feb 2 2011

ASJC Scopus subject areas

  • Biophysics

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