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Structure paper

TitleMolecular mechanism of actin filament elongation by formins.
Journal, issue, pagesScience, Vol. 384, Issue 6692, Page eadn9560, Year 2024
Publish dateApr 12, 2024
AuthorsWout Oosterheert / Micaela Boiero Sanders / Johanna Funk / Daniel Prumbaum / Stefan Raunser / Peter Bieling /
PubMed AbstractFormins 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 linksScience / PubMed:38603491
MethodsEM (single particle)
Resolution3.08 - 6.25 Å
Structure data

EMDB-19497: Cryo-EM reconstruction of the formin Cdc12 bound to the barbed end of F-actin (without phalloidin)
Method: EM (single particle) / Resolution: 4.54 Å

19499

8rty

EMDB-19499, PDB-8rty:
Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom
Method: EM (single particle) / Resolution: 6.25 Å

19501

8ru0

EMDB-19501, PDB-8ru0:
Structure of the undecorated barbed end of F-actin.
Method: EM (single particle) / Resolution: 3.08 Å

19503

8ru2

EMDB-19503, PDB-8ru2:
Structure of the F-actin barbed end bound by formin mDia1
Method: EM (single particle) / Resolution: 3.49 Å

19522

8rv2

EMDB-19522, PDB-8rv2:
Structure of the formin INF2 bound to the barbed end of F-actin.
Method: EM (single particle) / Resolution: 3.41 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

Source
  • homo sapiens (human)
  • schizosaccharomyces pombe (fission yeast)
  • amanita phalloides (death cap)
  • oryctolagus cuniculus (rabbit)
  • mus musculus (house mouse)
KeywordsSTRUCTURAL PROTEIN / actin / formin / Cdc12 / profilin / actin assembly / actin end / barbed end / INF2

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