Scientific article

Actin assembly requirements of the formin Fus1 to build the fusion focus

Published inJournal of cell science, vol. 135, no. 13, jcs260289
Publication date2022-07-01
First online date2022-07-08

In formin-family proteins, actin filament nucleation and elongation activities reside in the formin homology 1 (FH1) and FH2 domains, with reaction rates that vary by at least 20-fold between formins. Each cell expresses distinct formins that assemble one or several actin structures, raising the question of what confers each formin its specificity. Here, using the formin Fus1 in Schizosaccharomyces pombe, we systematically probed the importance of formin nucleation and elongation rates in vivo. Fus1 assembles the actin fusion focus, necessary for gamete fusion to form the zygote during sexual reproduction. By constructing chimeric formins with combinations of FH1 and FH2 domains previously characterized in vitro, we establish that changes in formin nucleation and elongation rates have direct consequences on fusion focus architecture, and that Fus1 native high nucleation and low elongation rates are optimal for fusion focus assembly. We further describe a point mutant in Fus1 FH2 that preserves native nucleation and elongation rates in vitro but alters function in vivo, indicating an additional FH2 domain property. Thus, rates of actin assembly are tailored for assembly of specific actin structures.

  • Actin cytoskeleton
  • Cell–cell fusion
  • Fission yeast Schizosaccharomyces pombe
  • Formin
Affiliation Not a UNIGE publication
Citation (ISO format)
BILLAULT-CHAUMARTIN, Ingrid et al. Actin assembly requirements of the formin Fus1 to build the fusion focus. In: Journal of cell science, 2022, vol. 135, n° 13, p. jcs260289. doi: 10.1242/jcs.260289
Main files (1)
Article (Published version)
ISSN of the journal0021-9533

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