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首页> 外文期刊>Cell motility and the cytoskeleton >Becoming stable and strong: the interplay between vinculin exchange dynamics and adhesion strength during adhesion site maturation.
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Becoming stable and strong: the interplay between vinculin exchange dynamics and adhesion strength during adhesion site maturation.

机译：变得稳定而强壮：粘附位点成熟过程中，纽蛋白交换动力学与粘附强度之间的相互作用。

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摘要

The coordinated formation and release of focal adhesions is necessary for cell attachment and migration. According to current models, these processes are caused by temporal variations in protein composition. Protein incorporation into focal adhesions is believed to be controlled by phosphorylation. Here, we tested the exchange dynamics of GFP-vinculin as marker protein of focal adhesions using the method of Fluorescence Recovery After Photobleaching. The relevance of the phosphorylation state of the protein, the age of focal adhesions and the acting force were investigated. For stable focal adhesions of stationary keratinocytes, we determined an exchangeable vinculin fraction of 52% and a recovery halftime of 57 s. Nascent focal adhesions of moving cells contained a fraction of exchanging vinculin of 70% with a recovery halftime of 36 s. Upon maturation, mean saturation values and recovery halftimes decreased to levels of 49% and 42 s, respectively. Additionally, the fraction of stably incorporated vinculin increased with cell forces and decreased with vinculin phosphorylation within these sites. Experiments on a nonphosphorylatable vinculin mutant construct at phosphorylation site tyr1065 confirmed the direct interplay between phosphorylation and exchange dynamics of adhesion proteins during adhesion site maturation.
机译：粘着斑的协调形成和释放对于细胞附着和迁移是必需的。根据当前模型，这些过程是由蛋白质组成的时间变化引起的。据信蛋白质结合到粘着斑中是通过磷酸化来控制的。在这里，我们使用荧光漂白后的荧光恢复方法测试了作为粘着斑标记蛋白的GFP-vinculin的交换动力学。研究了蛋白质的磷酸化状态，粘着斑的年龄和作用力的相关性。对于稳定的角质形成细胞的局灶性粘连，我们确定52％的可交换纽扣蛋白分数和57 s的恢复半衰期。运动细胞的新生粘着斑包含交换蛋白的比例为70％，恢复时间为36 s。成熟后，平均饱和度值和恢复半衰期分别降至49％和42 s。另外，在这些位点中，稳定掺入的纽蛋白的比例随着细胞力的增加而增加，并随着纽蛋白的磷酸化而降低。在磷酸化位点tyr1065上的非磷酸化纽扣蛋白突变体构建体的实验证实，在粘附位点成熟过程中，磷酸化与粘附蛋白的交换动力学之间具有直接的相互作用。

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