γ-Tubulin localizes at actin-based membrane protrusions and inhibits formation of stress-fibers

Biochem Biophys Res Commun. 2011 May 6;408(2):248-52. doi: 10.1016/j.bbrc.2011.04.007. Epub 2011 Apr 5.

Abstract

γ-Tubulin serves as a template in the γ-TuRC machinery to nucleate microtubules. Curiously, γ-tubulin also interacts with Arp2/3, a complex that nucleates actin filaments, and with the Arp2/3 activator WASH. We previously reported that γ-tubulin and Arp2/3 colocalize at the centrosome, where WASH localizes. Here, we report that γ-tubulin localizes at actin-based membrane protrusions, where Arp2/3 operates. This was confirmed by the presence of tagged γ-tubulin at membrane protrusions in stimulated cells and by downregulation of γ-tubulin expression. Surprisingly, expression of tagged γ-tubulin dramatically inhibited the formation of stress-fibers, while having no effect on microtubules. This phenotype is similar to the disruption of stress-fibers by the overexpression of the WCA domain of WASH and other Wiskott-Aldrich syndrome (WAS) family members. We hypothesize that γ-tubulin regulates Arp2/3 and actin nucleation promoting factors such as WASH, explaining the similar effect of γ-tubulin expression and WCA domain expression on stress-fibers. The data presented here indicate that γ-tubulin has a profound relationship with actin filament dynamics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin-Related Protein 2 / metabolism
  • Actin-Related Protein 3 / metabolism
  • Actins / metabolism*
  • Cell Line, Tumor
  • HeLa Cells
  • Humans
  • Stress Fibers / metabolism*
  • Tubulin / metabolism*

Substances

  • Actin-Related Protein 2
  • Actin-Related Protein 3
  • Actins
  • Tubulin