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Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.
Structural highlights
FunctionCDC12_SCHPO Plays a role in the cell cycle. Involved in cytokinesis. Component of the cell division ring. In the absence of profilin, caps the barbed end of actin filaments, thus preventing subunit addition and dissociation. In the presence of profilin, nucleates actin filaments that grow rapidly from their barbed ends.[1] Publication Abstract from PubMedFormins 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. Molecular mechanism of actin filament elongation by formins.,Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P Science. 2024 Apr 12;384(6692):eadn9560. doi: 10.1126/science.adn9560. Epub 2024 , Apr 12. PMID:38603491[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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