Arachidonic acid stimulates formation of a novel complex containing nucleolin and RhoA.
Arachidonic acid stimulates formation of a novel complex containing nucleolin and RhoA.
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DOI：
10.1016/j.febslet.2011.01.035
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发表时间：
2011-02-18
期刊：
影响因子：
3.5
通讯作者：
Roberts JD
中科院分区：
文献类型：
--
作者：
Garcia MC;Williams J;Johnson K;Olden K;Roberts JD
花生四烯酸（AA）通过p38丝裂原活化蛋白激酶介导的RhoA信号通路刺激细胞粘附。在这里，我们报告的蛋白质组学筛选后，AA-治疗确定核仁素，多功能核仁蛋白，在一个复杂的GTdR，RhoA，其中还包括Rho激酶，ROCK。AA刺激的细胞粘附被核仁素靶向shRNA的表达抑制，并且多蛋白复合物的形成被显性负性RhoA的表达阻断。AA处理还诱导核仁素的ROCK依赖性丝氨酸磷酸化和核仁素从细胞核到细胞质的易位，在那里它似乎与RhoA共定位。这些数据表明，存在一个新的信号通路，通过它的位置和翻译后状态的核仁素调制。
Arachidonic acid (AA) stimulates cell adhesion through a p38 mitogen activated protein kinase-mediated RhoA signaling pathway. Here we report that a proteomic screen following AA-treatment identified nucleolin, a multifunctional nucleolar protein, in a complex with the GTPase, RhoA, that also included the Rho kinase, ROCK. AA-stimulated cell adhesion was inhibited by expression of nucleolin-targeted shRNA and formation of the multiprotein complex was blocked by expression of dominant-negative RhoA. AA-treatment also induced ROCK-dependent serine phosphorylation of nucleolin and translocation of nucleolin from the nucleus to the cytoplasm, where it appeared to co-localize with RhoA. These data suggest the existence of a new signaling pathway through which the location and post-translational state of nucleolin are modulated.
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