Center for Cell Biology and Cancer Research, Albany Medical College, Albany, NY 12208, USA.
J Cell Sci. 2010 Jun 15;123(Pt 12):2094-102. doi: 10.1242/jcs.057505. Epub 2010 May 25.
Microtubules nucleated from gamma-tubulin ring complexes located at the centrosome regulate the localization of organelles, promote vesicular transport and direct cell migration. Although several signaling mechanisms have been identified that regulate microtubule dynamics during interphase, signaling pathways that promote microtubule nucleation remain elusive. We assayed microtubule regrowth following nocodazole washout in human fibroblasts and CHO-K1 cells adhered to fibronectin in either normal serum-free medium or the serum-free, growth-promoting medium, CCM1, which contains IGF1 and androgen, as well as other nutrients. The results indicate that integrin-mediated adhesion is not sufficient to promote rapid microtubule regrowth in either cell type. The addition of androgen, but not IGF1, for 5 minutes was sufficient to promote rapid regrowth and this occurred by a mechanism requiring the androgen receptor. Since Src is a component of the cytoplasmic androgen-receptor-signaling complex, we examined its role using Src siRNA, the Src kinase inhibitor SU6656, and the expression of a constitutively active Src mutant. The data show that Src signaling is both required and sufficient to promote rapid microtubule regrowth in cells adhered to fibronectin. Measurement of the density of microtubules close to the centrosome and the rates of GFP-EB1-labeled microtubules emanating from the centrosome indicated that Src signaling promotes microtubule nucleation. Furthermore, recovery of GFP-gamma-tubulin at the centrosome following photobleaching and measurements of endogenous gamma-tubulin levels at the centrosome showed that androgen and Src signaling regulate the levels of centrosomal gamma-tubulin. Thus, we propose that androgen and Src signaling regulate microtubule nucleation during interphase by promoting the centrosomal localization of gamma-tubulin.
微管由位于中心体的γ-微管蛋白环复合物组装而成,调节细胞器的定位,促进囊泡运输并指导细胞迁移。虽然已经确定了几种调节有丝分裂期间微管动力学的信号机制,但促进微管组装的信号途径仍然难以捉摸。我们在人成纤维细胞和附着在纤维连接蛋白上的 CHO-K1 细胞中检测了有丝分裂后微管的再生,这些细胞分别在正常无血清培养基或无血清促生长培养基 CCM1 中培养,CCM1 中含有 IGF1 和雄激素以及其他营养物质。结果表明,整合素介导的黏附不足以促进两种细胞类型中微管的快速再生。雄激素(而非 IGF1)的添加 5 分钟足以促进快速再生,该过程通过需要雄激素受体的机制发生。由于 Src 是细胞质雄激素受体信号复合物的组成部分,我们使用 Src siRNA、Src 激酶抑制剂 SU6656 和组成性激活的 Src 突变体来检查其作用。数据表明,Src 信号传导对于附着在纤维连接蛋白上的细胞中快速微管再生既需要又充分。靠近中心体的微管密度和从中心体发出的 GFP-EB1 标记的微管的速率的测量表明,Src 信号传导促进了微管的组装。此外,在用光漂白使 GFP-γ-微管蛋白在中心体上失活后观察到 GFP-γ-微管蛋白在中心体上的恢复以及对中心体上内源性 γ-微管蛋白水平的测量表明,雄激素和 Src 信号传导调节中心体 γ-微管蛋白的水平。因此,我们提出雄激素和 Src 信号传导通过促进中心体 γ-微管蛋白的定位来调节有丝分裂期间的微管组装。