Profilin regulates F-Actin network homeostasis by favoring formin over Arp2/3 complex

Cristian Suarez, Robert T. Carroll, Thomas A. Burke, Jenna R. Christensen, Andrew J. Bestul, Jennifer A. Sees, Michael L. James, Vladimir Sirotkin*, David R. Kovar

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

185 Scopus citations


Fission yeast cells use Arp2/3 complex and formin to assemble diverse filamentous actin (F-actin) networks within a common cytoplasm for endocytosis, division, and polarization. Although these homeostatic F-actin networks are usually investigated separately, competition for a limited pool of actin monomers (G-actin) helps to regulate their size anddensity. However, the mechanism by which G-actinis correctly distributed between rival F-actin networks is not clear. Using a combination of cell biological approaches and invitro reconstitution of competition between actin assembly factors, we found that the small G-actin binding protein profilin directly inhibits Arp2/3 complex-mediated actin assembly. Profilin is therefore required for formin to compete effectively with excess Arp2/3 complex for limited G-actin and to assemble F-actin for contractile ring formation in dividing cells.

Original languageEnglish (US)
Pages (from-to)43-53
Number of pages11
JournalDevelopmental Cell
Issue number1
StatePublished - 2015

ASJC Scopus subject areas

  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • Developmental Biology
  • Cell Biology


Dive into the research topics of 'Profilin regulates F-Actin network homeostasis by favoring formin over Arp2/3 complex'. Together they form a unique fingerprint.

Cite this