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首页> 外文期刊>Cell motility and the cytoskeleton >GEF at work: Vav in protruding filopodia.
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GEF at work: Vav in protruding filopodia.

机译：全球环境基金正在开展工作：突出型丝状伪足的Vav。

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摘要

The Dbl family proto-oncogene vav is a nucleotide exchange factor for Rho family GTPases and is involved in triggering cytoskeletal changes contributing to the alterations of cell shape and motility, as well as in the induction of gene expression. In vitro and in vivo Vav is regulated by multiple tyrosine phosphorylation and binding to phosphatidylinositol phosphates. Although recruitment of Vav to the plasma membrane appears important for the activation of Vav function, there is little information on the precise subcellular localization of Vav in living cells. Employing live video fluorescence and immunoelectron microscopy, we show that GFP-tagged full-length Vav, and several mutants in which the N-terminal regulatory calponin homology (CH) domain has been deleted, specifically localize to the tips of filopodia. This localization was congruent with a high content of tyrosine phosphorylation in these regions. Consistent with earlier observations, mutants lacking the C-terminal SH domain region were unable to translocate to the filopodia tips. The enrichment in filopodial tips persisted despite their lateral movement but was dependent on forward growth. Upon retraction, the signal was rapidly lost, indicating that Vav undergoes a specific and transient translocation in response to actin-based, protrusive events in filopodia. Copyright 2001 Wiley-Liss, Inc.
机译：Dbl家族原癌基因vav是Rho家族GTPases的核苷酸交换因子，参与触发细胞骨架变化，从而有助于细胞形状和运动的改变，以及诱导基因表达。在体外和体内，Vav通过多个酪氨酸磷酸化和与磷脂酰肌醇磷酸酯的结合来调节。尽管将Vav募集到质膜似乎对激活Vav功能很重要，但是关于Vav在活细胞中的精确亚细胞定位的信息很少。利用实时视频荧光和免疫电子显微镜，我们显示了GFP标记的全长Vav，以及其中N末端调节钙蛋白同源性（CH）域已被删除的几个突变体，特别是定位于丝状伪足的尖端。在这些区域中，这种定位与酪氨酸磷酸化的高含量是一致的。与早期的观察结果一致，缺乏C末端SH结构域区域的突变体无法转移到丝状伪足尖端。尽管有侧向运动，但在尾足尖端的富集仍然持续，但取决于向前生长。缩回后，信号迅速丢失，表明Vav响应丝状伪足中基于肌动蛋白的突出事件而经历了特定且短暂的移位。版权所有2001 Wiley-Liss，Inc.

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