2.50
Hdl Handle:
http://hdl.handle.net/10033/70575
Title:
F- and G-actin concentrations in lamellipodia of moving cells.
Authors:
Koestler, Stefan A; Rottner, Klemens; Lai, Frank; Block, Jennifer; Vinzenz, Marlene; Small, J Victor
Abstract:
Cells protrude by polymerizing monomeric (G) into polymeric (F) actin at the tip of the lamellipodium. Actin filaments are depolymerized towards the rear of the lamellipodium in a treadmilling process, thereby supplementing a G-actin pool for a new round of polymerization. In this scenario the concentrations of F- and G-actin are principal parameters, but have hitherto not been directly determined. By comparing fluorescence intensities of bleached and unbleached regions of lamellipodia in B16-F1 mouse melanoma cells expressing EGFP-actin, before and after extraction with Triton X-100, we show that the ratio of F- to G-actin is 3.2+/-0.9. Using electron microscopy to determine the F-actin content, this ratio translates into F- and G-actin concentrations in lamellipodia of approximately 500 microM and 150 microM, respectively. The excess of G-actin, at several orders of magnitude above the critical concentrations at filament ends indicates that the polymerization rate is not limited by diffusion and is tightly controlled by polymerization/depolymerization modulators.
Affiliation:
Institute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna, Austria.
Citation:
F- and G-actin concentrations in lamellipodia of moving cells. 2009, 4 (3):e4810 PLoS ONE
Journal:
PloS one
Issue Date:
2009
URI:
http://hdl.handle.net/10033/70575
DOI:
10.1371/journal.pone.0004810
PubMed ID:
19277198
Type:
Article
Language:
en
ISSN:
1932-6203
Appears in Collections:
Publications of RG Cytoskeleton Dynamics (CYD)

Full metadata record

DC FieldValue Language
dc.contributor.authorKoestler, Stefan A-
dc.contributor.authorRottner, Klemens-
dc.contributor.authorLai, Frank-
dc.contributor.authorBlock, Jennifer-
dc.contributor.authorVinzenz, Marlene-
dc.contributor.authorSmall, J Victor-
dc.date.accessioned2009-06-16T13:02:06Z-
dc.date.available2009-06-16T13:02:06Z-
dc.date.issued2009-
dc.identifier.citationF- and G-actin concentrations in lamellipodia of moving cells. 2009, 4 (3):e4810 PLoS ONEen
dc.identifier.issn1932-6203-
dc.identifier.pmid19277198-
dc.identifier.doi10.1371/journal.pone.0004810-
dc.identifier.urihttp://hdl.handle.net/10033/70575-
dc.description.abstractCells protrude by polymerizing monomeric (G) into polymeric (F) actin at the tip of the lamellipodium. Actin filaments are depolymerized towards the rear of the lamellipodium in a treadmilling process, thereby supplementing a G-actin pool for a new round of polymerization. In this scenario the concentrations of F- and G-actin are principal parameters, but have hitherto not been directly determined. By comparing fluorescence intensities of bleached and unbleached regions of lamellipodia in B16-F1 mouse melanoma cells expressing EGFP-actin, before and after extraction with Triton X-100, we show that the ratio of F- to G-actin is 3.2+/-0.9. Using electron microscopy to determine the F-actin content, this ratio translates into F- and G-actin concentrations in lamellipodia of approximately 500 microM and 150 microM, respectively. The excess of G-actin, at several orders of magnitude above the critical concentrations at filament ends indicates that the polymerization rate is not limited by diffusion and is tightly controlled by polymerization/depolymerization modulators.en
dc.language.isoenen
dc.titleF- and G-actin concentrations in lamellipodia of moving cells.en
dc.typeArticleen
dc.contributor.departmentInstitute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna, Austria.en
dc.identifier.journalPloS oneen

Related articles on PubMed

This item is licensed under a Creative Commons License
Creative Commons
All Items in HZI are protected by copyright, with all rights reserved, unless otherwise indicated.