Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
- PMID: 10524632
- DOI: 10.1038/44183
Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
Abstract
Actin polymerization is essential for cell locomotion and is thought to generate the force responsible for cellular protrusions. The Arp2/3 complex is required to stimulate actin assembly at the leading edge in response to signalling. The bacteria Listeria and Shigella bypass the signalling pathway and harness the Arp2/3 complex to induce actin assembly and to propel themselves in living cells. However, the Arp2/3 complex alone is insufficient to promote movement. Here we have used pure components of the actin cytoskeleton to reconstitute sustained movement in Listeria and Shigella in vitro. Actin-based propulsion is driven by the free energy released by ATP hydrolysis linked to actin polymerization, and does not require myosin. In addition to actin and activated Arp2/3 complex, actin depolymerizing factor (ADF, or cofilin) and capping protein are also required for motility as they maintain a high steady-state level of G-actin, which controls the rate of unidirectional growth of actin filaments at the surface of the bacterium. The movement is more effective when profilin, alpha-actinin and VASP (for Listeria) are also included. These results have implications for our understanding of the mechanism of actin-based motility in cells.
Comment in
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Cell motility. Bare bones of the cytoskeleton.Nature. 1999 Oct 7;401(6753):542-3. doi: 10.1038/44044. Nature. 1999. PMID: 10524617 No abstract available.
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