Reference - PMID:38603491 - Molecular mechanism of actin filament elongation by formins.
Reference summary
- PubMed ID
- PMID:38603491
- Title
- Molecular mechanism of actin filament elongation by formins.
- Authors
- Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P
- Citation
- Science 2024 Apr 12;384(6692):eadn9560
- Publication year
- 2024
- Abstract
- Formins control the assembly of actin filaments (F-actin) that drive cell morphogenesis and motility in eukaryotes. However, their molecular interaction with F-actin and their mechanism of action remain unclear. In this work, we present high-resolution cryo-electron microscopy structures of F-actin barbed ends bound by three distinct formins, revealing a common asymmetric formin conformation imposed by the filament. Formation of new intersubunit contacts during actin polymerization sterically displaces formin and triggers its translocation. This "undock-and-lock" mechanism explains how actin-filament growth is coordinated with formin movement. Filament elongation speeds are controlled by the positioning and stability of actin-formin interfaces, which distinguish fast and slow formins. Furthermore, we provide a structure of the actin-formin-profilin ring complex, which resolves how profilin is rapidly released from the barbed end during filament elongation.
