Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis

Nicola Tolliday, Lynn VerPlank, Rong Li

Research output: Contribution to journalArticlepeer-review

110 Scopus citations


In eukaryotic cells, dynamic rearrangement of the actin cytoskeleton is critical for cell division. In the yeast Saccharomyces cerevisiae, three main structures constitute the actin cytoskeleton: cortical actin patches, cytoplasmic actin cables, and the actin-based cytokinetic ring [1-4]. The conserved Arp2/3 complex and a WASP-family protein mediate actin patch formation, whereas the yeast formins (Bni1 and Bnr1) promote assembly of actin cables [5-9]. However, the mechanism of actin ring formation is currently unclear. Here, we show that actin filaments are required for cytokinesis in S. cerevisiae, and that the actin ring is a highly dynamic structure that undergoes constant turnover. Assembly of the actin ring requires the formin-like proteins and profilin, but is not Arp2/3-mediated. Furthermore, the formin-dependent actin ring assembly pathway is regulated by the Rho-type GTPase Rho1 but not Cdc42. Finally, we show that the formins are not required for localization of Cyk1/Iqg1, an IQGAP-like protein previously shown to be required for actin ring formation, suggesting that formin-like proteins and Cyk1 act synergistically but independently in assembly of the actin ring.

Original languageEnglish (US)
Pages (from-to)1864-1870
Number of pages7
JournalCurrent Biology
Issue number21
StatePublished - Oct 29 2002
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)


Dive into the research topics of 'Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis'. Together they form a unique fingerprint.

Cite this