Core Unit Chip Application (CUCA), Institute of Human Genetics and Anthropology, University Hospital Jena, Jena, Germany.
Exp Cell Res. 2010 Apr 15;316(7):1234-40. doi: 10.1016/j.yexcr.2010.01.022. Epub 2010 Jan 25.
Actin structures are involved in several biological processes and the disruption of actin polymerisation induces impaired motility of eukaryotic cells. Different factors are involved in regulation and maintenance of the cytoskeletal actin architecture. Here we show that S100A10 participates in the particular organisation of actin filaments. Down-regulation of S100A10 by specific siRNA triggered a disorganisation of filamentous actin structures without a reduction of the total cellular actin concentration. In contrast, the formation of cytoskeleton structures containing tubulin was unhindered in S100A10 depleted cells. Interestingly, the cellular distribution of annexin A2, an interaction partner of S100A10, was unaffected in S100A10 depleted cells. Cells lacking S100A10 showed an impaired migration activity and were unable to close a scratched wound. Our data provide first insights of S100A10 function as a regulator of the filamentous actin network.
肌动蛋白结构参与了多种生物过程，肌动蛋白聚合的破坏会导致真核细胞运动能力受损。不同的因素参与了细胞骨架肌动蛋白结构的调节和维持。在这里，我们表明 S100A10 参与了肌动蛋白丝的特定组织。通过特异性 siRNA 下调 S100A10 会引发丝状肌动蛋白结构的紊乱，而不会减少总细胞肌动蛋白浓度。相比之下，在 S100A10 耗尽的细胞中，包含微管的细胞骨架结构的形成不受阻碍。有趣的是，S100A10 耗尽的细胞中，S100A10 的相互作用伙伴 annexin A2 的细胞分布不受影响。缺乏 S100A10 的细胞迁移活性受损，无法封闭划痕伤口。我们的数据首次提供了 S100A10 作为丝状肌动蛋白网络调节剂的功能见解。
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