The nature of the globular- to fibrous-actin transition

Toshiro Oda (), Mitsusada Iwasa, Tomoki Aihara, Yuichiro Maéda and Akihiro Narita
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Toshiro Oda: X-ray Structural Analysis Research Team, RIKEN SPring-8 Center, RIKEN Harima Institute, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan
Mitsusada Iwasa: ERATO project ‘Actin-filament dynamics’, Japan Science and Technology Agency (JST), 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan
Tomoki Aihara: X-ray Structural Analysis Research Team, RIKEN SPring-8 Center, RIKEN Harima Institute, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan
Yuichiro Maéda: ERATO project ‘Actin-filament dynamics’, Japan Science and Technology Agency (JST), 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan
Akihiro Narita: Graduate School of Science, Nagoya University, Furo, Nagoya 464-8601, Japan

Nature, 2009, vol. 457, issue 7228, 441-445

Abstract: 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 Å in the radial direction and 5.6 Å 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.

Date: 2009
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DOI: 10.1038/nature07685

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