Article
- The EMBO Journal (2007) 26, 4597 - 4606
- doi:10.1038/sj.emboj.7601874
Published online: 4 October 2007
Subject Categories:
Structural basis for the recruitment of profilin–actin complexes during filament elongation by Ena/VASP
François Ferron1, Grzegorz Rebowski1, Sung Haeng Lee1 and Roberto Dominguez1
- Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA, USA
Correspondence to:
Roberto Dominguez, Department of Physiology, University of Pennsylvania School of Medicine, A507 Richards Building, 3700 Hamilton Walk, Philadelphia, PA 19104-6058, USA. Tel.: +1 215 573 4559; Fax: +1 215 573 5851; E-mail: droberto@mail.med.upenn.edu
Received 18 July 2007; Accepted 10 September 2007
Abstract
Cells sustain high rates of actin filament elongation by maintaining a large pool of actin monomers above the critical concentration for polymerization. Profilin–actin complexes constitute the largest fraction of polymerization-competent actin monomers. Filament elongation factors such as Ena/VASP and formin catalyze the transition of profilin–actin from the cellular pool onto the barbed end of growing filaments. The molecular bases of this process are poorly understood. Here we present structural and energetic evidence for two consecutive steps of the elongation mechanism: the recruitment of profilin–actin by the last poly-Pro segment of vasodilator-stimulated phosphoprotein (VASP) and the binding of profilin–actin simultaneously to this poly-Pro and to the G-actin-binding (GAB) domain of VASP. The actin monomer bound at the GAB domain is proposed to be in position to join the barbed end of the growing filament concurrently with the release of profilin.
Keywords:
- actin,
- cytoskeleton dynamics,
- filament elongation,
- profilin
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