Beta-actin mRNA localization is regulated by signal transduction mechanisms

Beta-actin mRNA localization is regulated by signal transduction mechanisms
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β-肌动蛋白 mRNA 定位受信号转导机制调节

DOI:
--
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发表时间:
1994
影响因子:
7.8
通讯作者:
A. Ross
A. Ross
中科院分区:
生物学1区
文献类型:
--
作者:
V. Latham;E. Kislauskis;R. Singer;A. Ross

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-肌动蛋白mRNA定位于鸡胚成纤维细胞(CEFs)的前叶(Lawrence, J.和R. Singer. 1986)。细胞。45:407- 415),靠近板足肌动蛋白聚合驱动细胞运动的地方。在血清饥饿期间-肌动蛋白mRNA变得弥漫性和非局部化。添加FCS诱导β -肌动蛋白mRNA在2-5分钟内快速重新分布到前导片中。PDGF(一种成纤维细胞趋化因子)也出现了类似的分布。pdgf诱导的β -肌动蛋白mRNA再分配被酪氨酸激酶抑制剂herbimycin抑制,表明这一过程需要完整的酪氨酸激酶活性,类似于肌动蛋白丝聚合和趋化性。溶血磷脂酸,已被证明能迅速诱导肌动蛋白应激纤维的形成(Ridley, A.和A. Hall, 1992)。细胞。790:389-399),也增加了外周β -肌动蛋白mRNA在几分钟内的定位。这表明肌动蛋白聚合和mRNA定位可能受到类似信号通路的调控。此外,激酶A或C的激活剂或抑制剂也可以使血清中生长的细胞中的稳态β -肌动蛋白mRNA离域,并可以抑制血清饥饿CEFs中外周定位β -肌动蛋白mRNA的血清诱导。这些数据表明,生理相关的细胞外因子通过信号转导途径可以调节肌动蛋白合成的空间位点,进而影响细胞极性和运动性。
Beta-actin mRNA is localized in the leading lamellae of chicken embryo fibroblasts (CEFs) (Lawrence, J., and R. Singer. 1986. Cell. 45:407- 415), close to where actin polymerization in the lamellipodia drives cellular motility. During serum starvation beta-actin mRNA becomes diffuse and non-localized. Addition of FCS induces a rapid (within 2-5 min) redistribution of beta-actin mRNA into the leading lamellae. A similar redistribution was seen with PDGF, a fibroblast chemotactic factor. PDGF-induced beta-actin mRNA redistribution was inhibited by the tyrosine kinase inhibitor herbimycin, indicating that this process requires intact tyrosine kinase activity, similar to actin filament polymerization and chemotaxis. Lysophosphatidic acid, which has been shown to rapidly induce actin stress fiber formation (Ridley, A., and A. Hall. 1992. Cell. 790:389-399), also increases peripheral beta-actin mRNA localization within minutes. This suggests that actin polymerization and mRNA localization may be regulated by similar signaling pathways. Additionally, activators or inhibitors of kinase A or C can also delocalize steady-state beta-actin mRNA in cells grown in serum, and can inhibit the serum induction of peripherally localized beta-actin mRNA in serum-starved CEFs. These data show that physiologically relevant extracellular factors operating through a signal transduction pathway can regulate spatial sites of actin protein synthesis, which may in turn affect cellular polarity and motility.
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