Structural basis for polarized elongation of actin filaments.

Proceedings of the National Academy of Sciences of the United States of America
Vilmos ZsolnayGregory A Voth

Abstract

Actin filaments elongate and shorten much faster at their barbed end than their pointed end, but the molecular basis of this difference has not been understood. We use all-atom molecular dynamics simulations to investigate the properties of subunits at both ends of the filament. The terminal subunits tend toward conformations that resemble actin monomers in solution, while contacts with neighboring subunits progressively flatten the conformation of internal subunits. At the barbed end the terminal subunit is loosely tethered by its DNase-1 loop to the third subunit, because its monomer-like conformation precludes stabilizing contacts with the penultimate subunit. The motions of the terminal subunit make the partially flattened penultimate subunit accessible for binding monomers. At the pointed end, unique contacts between the penultimate and terminal subunits are consistent with existing cryogenic electron microscopic (cryo-EM) maps, limit binding to incoming monomers, and flatten the terminal subunit, which likely promotes ATP hydrolysis and rapid phosphate release. These structures explain the distinct polymerization kinetics of the two ends.

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Citations

Nov 8, 2020·Current Opinion in Cell Biology·Antoine Jégou, Guillaume Romet-Lemonne
Aug 24, 2021·Frontiers of Physics·Nicholas CastanedaEllen Hyeran Kang
Sep 13, 2021·Biophysical Journal·Aaron D RosenbloomThomas D Pollard

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