Abstract
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 language | English (US) |
|---|---|
| Pages (from-to) | 1864-1870 |
| Number of pages | 7 |
| Journal | Current Biology |
| Volume | 12 |
| Issue number | 21 |
| DOIs | |
| State | Published - Oct 29 2002 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
Cite this
Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis. / Tolliday, Nicola; VerPlank, Lynn; Li, Rong.
In: Current Biology, Vol. 12, No. 21, 29.10.2002, p. 1864-1870.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis
AU - Tolliday, Nicola
AU - VerPlank, Lynn
AU - Li, Rong
PY - 2002/10/29
Y1 - 2002/10/29
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0037195254&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037195254&partnerID=8YFLogxK
U2 - 10.1016/S0960-9822(02)01238-1
DO - 10.1016/S0960-9822(02)01238-1
M3 - Article
C2 - 12419188
AN - SCOPUS:0037195254
VL - 12
SP - 1864
EP - 1870
JO - Current Biology
JF - Current Biology
SN - 0960-9822
IS - 21
ER -