Mechanisms of formin-mediated actin assembly and dynamics

Research output: Contribution to journalReview articlepeer-review

81 Scopus citations


Cellular viability requires tight regulation of actin cytoskeletal dynamics. Distinct families of nucleation-promoting factors enable the rapid assembly of filament nuclei that elongate and are incorporated into diverse and specialized actin-based structures. In addition to promoting filament nucleation, the formin family of proteins directs the elongation of unbranched actin filaments. Processive association of formins with growing filament ends is achieved through continuous barbed end binding of the highly conserved, dimeric formin homology (FH) 2 domain. In cooperation with the FH1 domain and C-terminal tail region, FH2 dimers mediate actin subunit addition at speeds that can dramatically exceed the rate of spontaneous assembly. Here, I review recent biophysical, structural, and computational studies that have provided insight into the mechanisms of formin-mediated actin assembly and dynamics.

Original languageEnglish (US)
Pages (from-to)1553-1569
Number of pages17
JournalBiophysical Reviews
Issue number6
StatePublished - Dec 1 2018

Bibliographical note

Publisher Copyright:
© 2018, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature.


  • Actin
  • Formin
  • Polymerization
  • Profilin


Dive into the research topics of 'Mechanisms of formin-mediated actin assembly and dynamics'. Together they form a unique fingerprint.

Cite this