The nature of the globular- to fibrous-actin transition - PubMed (original) (raw)
. 2009 Jan 22;457(7228):441-5.
doi: 10.1038/nature07685.
Affiliations
- PMID: 19158791
- DOI: 10.1038/nature07685
The nature of the globular- to fibrous-actin transition
Toshiro Oda et al. Nature. 2009.
Erratum in
- Nature. 2009 Sep 24;461(7263):550
Abstract
Actin plays crucial parts in cell motility through a dynamic process driven by polymerization and depolymerization, that is, the globular (G) to fibrous (F) actin transition. Although our knowledge about the actin-based cellular functions and the molecules that regulate the G- to F-actin transition is growing, the structural aspects of the transition remain enigmatic. We created a model of F-actin using X-ray fibre diffraction intensities obtained from well oriented sols of rabbit skeletal muscle F-actin to 3.3 A in the radial direction and 5.6 A along the equator. Here we show that the G- to F-actin conformational transition is a simple relative rotation of the two major domains by about 20 degrees. As a result of the domain rotation, the actin molecule in the filament is flat. The flat form is essential for the formation of stable, helical F-actin. Our F-actin structure model provides the basis for understanding actin polymerization as well as its molecular interactions with actin-binding proteins.
Comment in
- Structural biology: actin in a twist.
Holmes KC. Holmes KC. Nature. 2009 Jan 22;457(7228):389-90. doi: 10.1038/457389a. Nature. 2009. PMID: 19158779 No abstract available.
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References
- Science. 2001 Jul 27;293(5530):708-11 - PubMed
- J Biol Chem. 2008 Jul 25;283(30):21045-53 - PubMed
- Nature. 1990 Sep 6;347(6288):37-44 - PubMed
- Annu Rev Biochem. 2006;75:467-92 - PubMed
- J Biol Chem. 1992 May 5;267(13):9326-30 - PubMed
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