Department of Medical Protein Research, VIB, B-9000 Ghent, Belgium.
Biochem Biophys Res Commun. 2011 May 6;408(2):248-52. doi: 10.1016/j.bbrc.2011.04.007. Epub 2011 Apr 5.
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.
γ-微管蛋白作为 γ-TuRC 机器中的模板,启动微管的形成。奇怪的是,γ-微管蛋白还与 Arp2/3 相互作用,Arp2/3 是一种启动肌动蛋白丝形成的复合物,并且与 Arp2/3 激活因子 WASH 相互作用。我们之前报道过,γ-微管蛋白和 Arp2/3 在中心体共定位,WASH 也在中心体定位。在这里,我们报告说γ-微管蛋白定位于肌动蛋白为基础的膜突中,而 Arp2/3 在该处起作用。这一点在受刺激的细胞中标记的 γ-微管蛋白存在于膜突中得到了证实,并且下调了 γ-微管蛋白的表达。令人惊讶的是,标记的 γ-微管蛋白的表达显著抑制了应激纤维的形成,而对微管没有影响。这种表型与 WASH 的 WCA 结构域和其他 Wiskott-Aldrich 综合征 (WAS) 家族成员的过表达对应激纤维的破坏相似。我们假设 γ-微管蛋白调节 Arp2/3 和肌动蛋白成核促进因子,如 WASH,这解释了 γ-微管蛋白表达和 WCA 结构域表达对应激纤维的相似影响。这里呈现的数据表明,γ-微管蛋白与肌动蛋白丝动力学有很深的关系。