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-Structure paper
Title | Molecular mechanism of actin filament elongation by formins. |
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Journal, issue, pages | Science, Vol. 384, Issue 6692, Page eadn9560, Year 2024 |
Publish date | Apr 12, 2024 |
Authors | Wout Oosterheert / Micaela Boiero Sanders / Johanna Funk / Daniel Prumbaum / Stefan Raunser / Peter Bieling / |
PubMed 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 ...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. |
External links | Science / PubMed:38603491 |
Methods | EM (single particle) |
Resolution | 3.08 - 6.25 Å |
Structure data | EMDB-19496, PDB-8rtt: EMDB-19497: Cryo-EM reconstruction of the formin Cdc12 bound to the barbed end of F-actin (without phalloidin) EMDB-19499, PDB-8rty: EMDB-19501, PDB-8ru0: EMDB-19503, PDB-8ru2: EMDB-19522, PDB-8rv2: |
Chemicals | ChemComp-ADP: ChemComp-MG: ChemComp-PO4: ChemComp-ATP: |
Source |
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Keywords | STRUCTURAL PROTEIN / actin / formin / Cdc12 / actin assembly. / profilin / actin assembly / actin end / barbed end / INF2 |