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

Takanori Otomo, Diana R. Tomchick, Chinatsu Otomo, Sanjay C. Panchal, Mischa Machius and Michael K. Rosen ()
Additional contact information
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

Nature, 2005, vol. 433, issue 7025, 488-494

Abstract: 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.

Date: 2005
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature03251 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:433:y:2005:i:7025:d:10.1038_nature03251

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature03251

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().