Distinct VASP tetramers synergize in the processive elongation of individual actin filaments from clustered arrays.

ABSTRACT: Ena/VASP proteins act as actin polymerases that drive the processive elongation of filament barbed ends in membrane protrusions or at the surface of bacterial pathogens. Based on previous analyses of fast and slow elongating VASP proteins by in vitro total internal reflection fluorescence microscopy (TIRFM) and kinetic and thermodynamic measurements, we established a kinetic model of Ena/VASP-mediated actin filament elongation. At steady state, it entails that tetrameric VASP uses one of its arms to processively track growing filament barbed ends while three G-actin-binding sites (GABs) on other arms are available to recruit and deliver monomers to the filament tip, suggesting that VASP operates as a single tetramer in solution or when clustered on a surface, albeit processivity and resist

SUBMITTER: Bruhmann S 

PROVIDER: S-EPMC5530675 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature