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首页> 外文期刊>Molecular biology of the cell >RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic cell migration via its Src-binding site
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RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic cell migration via its Src-binding site

机译：RACK1通过其Src结合位点调节整合素介导的粘附，突出和趋化性细胞迁移

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Mammalian cDNA expression cloning was used to identify novel regulators of integrin-mediated cell-substratum adhesions. Using a focal adhesion morphology screen, we identified a cDNA with homology to a receptor for activated protein kinase C (RACK1) that induced a loss of central focal adhesions and stress fibers in CHO-K1 cells. The identified cDNA was a C-terminal truncated form of RACK1 that had one of the putative protein kinase C binding sites but lacked the region proposed to bind the beta integrin cytoplasmic domain and the tyrosine kinase Src. To investigate the role of RACK1 during cell spreading and migration, we tagged RACK1, a C-terminal truncated RACK1 and a point mutant that does not bind Src (RACK Y246F) with green fluorescent protein and expressed them in CHO-K1 cells. We found that RACK1 regulates the organization of focal adhesions and that it localizes to a subset of nascent focal complexes in areas of protrusion that contain paxillin but not vinculin. We also found that RACK1 regulates cell protrusion and chemotactic migration through its Src binding site. Together, these findings suggest that RACK1 regulates adhesion, protrusion, and chemotactic migration through its interaction with Src. [References: 39]
机译：哺乳动物cDNA表达克隆被用来识别整合素介导的细胞-基质粘附的新型调节剂。使用粘着斑形态学筛选，我们鉴定出与激活蛋白激酶C（RACK1）受体具有同源性的cDNA，该蛋白诱导CHO-K1细胞中中央粘着斑和应力纤维的丢失。鉴定的cDNA是RACK1的C端截短形式，具有一个假定的蛋白激酶C结合位点，但缺乏提议的结合β整联蛋白胞质结构域和酪氨酸激酶Src的区域。为了研究RACK1在细胞扩散和迁移中的作用，我们标记了RACK1，一个C端截短的RACK1和一个不与绿色荧光蛋白结合Src（RACK Y246F）的点突变体，并在CHO-K1细胞中表达了它们。我们发现，RACK1调节着灶性粘连的组织，并且它定位在含有paxillin但不包含长春花素的突起区域中新生的一个新的灶性复合物的子集。我们还发现RACK1通过其Src结合位点调节细胞突起和趋化性迁移。总之，这些发现表明RACK1通过与Src的相互作用来调节粘附，突出和趋化性迁移。 [参考：39]

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