Journal article
The reconstitution of actin polymerization on liposomes
Methods in molecular biology (Clifton, N.J.), Vol.606, pp.95-103
2010
DOI: 10.1007/978-1-60761-447-0_8
PMID: 20013392
Abstract
Membrane-associated actin polymerization is of considerable interest due to its role in cell migration and the motility of intracellular organelles. Intensive research efforts are underway to investigate the physiological role of membrane-associated actin as well as the regulation and mechanics of actin assembly. Branched actin polymerization on membranes is catalyzed by the Arp2/3 complex. Signaling events leading to the activation of the guanosine triphosphate (GTP)-binding protein Cdc42 stimulate Arp2/3-dependent actin polymerization. We have studied the role of Cdc42 at the Golgi apparatus in part by reconstituting actin polymerization on isolated Golgi membranes and on liposomes. In this manner, we showed that cytosolic proteins are sufficient for actin assembly on a phospholipid bilayer. Here we describe methods for the cell-free reconstitution of membrane-associated actin polymerization using liposomes and brain cytosol.
Details
- Title: Subtitle
- The reconstitution of actin polymerization on liposomes
- Creators
- Mark Stamnes - Department of Molecular Physiology & Biophysics, University of Iowa, Iowa City, USAWeidong Xu
- Resource Type
- Journal article
- Publication Details
- Methods in molecular biology (Clifton, N.J.), Vol.606, pp.95-103
- Publisher
- United States
- DOI
- 10.1007/978-1-60761-447-0_8
- PMID
- 20013392
- eISBN
- 9781607614470; 1607614472
- ISSN
- 1064-3745
- eISSN
- 1940-6029
- Grant note
- R01 GM068674 / NIGMS NIH HHS
- Language
- English
- Date published
- 2010
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984025365502771
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