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Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain

Author

Listed:
  • Takanori Otomo

    (University of Texas Southwestern Medical Center at Dallas)

  • Diana R. Tomchick

    (University of Texas Southwestern Medical Center at Dallas)

  • Chinatsu Otomo

    (University of Texas Southwestern Medical Center at Dallas)

  • Sanjay C. Panchal

    (University of Texas Southwestern Medical Center at Dallas)

  • Mischa Machius

    (University of Texas Southwestern Medical Center at Dallas)

  • Michael K. Rosen

    (University of Texas Southwestern Medical Center at Dallas)

Abstract

The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine–actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.

Suggested Citation

  • Takanori Otomo & Diana R. Tomchick & Chinatsu Otomo & Sanjay C. Panchal & Mischa Machius & Michael K. Rosen, 2005. "Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain," Nature, Nature, vol. 433(7025), pages 488-494, February.
    • Handle: RePEc:nat:nature:v:433:y:2005:i:7025:d:10.1038_nature03251
    DOI: 10.1038/nature03251
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    Cited by:

    1. Noura Alzahofi & Tobias Welz & Christopher L. Robinson & Emma L. Page & Deborah A. Briggs & Amy K. Stainthorp & James Reekes & David A. Elbe & Felix Straub & Wouter W. Kallemeijn & Edward W. Tate & Ph, 2020. "Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins," Nature Communications, Nature, vol. 11(1), pages 1-21, December.
    2. Riya Shah & Thomas C. Panagiotou & Gregory B. Cole & Trevor F. Moraes & Brigitte D. Lavoie & Christopher A. McCulloch & Andrew Wilde, 2024. "The DIAPH3 linker specifies a β-actin network that maintains RhoA and Myosin-II at the cytokinetic furrow," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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