Self-assembly of Actin Scaffolds at Ponticulin-containing Supported Phospholipid Bilayers.
Biophysical journal
- Publish Date: Feb 2006
- ISSN: 0006-3495
- Volume: 90
- Issue: 3
- Pages: L21-3
- Medium: Print
- Language: English
- Citation (JAMA): Johnson Benjamin R G, Bushby Richard J, Colyer John, et al. Self-assembly of Actin Scaffolds at Ponticulin-containing Supported Phospholipid Bilayers.. Biophys. J. Feb 2006;90:L21-3
Abstract
Phospholipid vesicles containing ponticulin have been used to form solid supported and tethered bilayer lipid membranes. The ponticulin serves as both a nucleation site for actin polymerization as well as a binding site for F-actin. Studies of F-actin binding to such bilayers have demonstrated the formation of an in vitro actin scaffold. The dissociation constant for the binding of F-actin filaments to a ponticulin-containing tethered bilayer was found to be 11 +/- 5 nM, indicative of high affinity binding.
Mesh Headings (Keywords): Actins, Animals, Binding Sites, Biophysics, Carrier Proteins, Dictyostelium, Lipid Bilayers, Lipids, Microfilament Proteins, Microscopy, Electron, Transmission, Models, Biological, Phosphatidylcholines, Phospholipids, Protein Binding
Check for Full Text / PubMed Unique Identifier (PMID): 16326915
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