Codependent functions of RSK2 and the apoptosis-promoting factor TIA-1 in stress granule assembly and cell survival.
Codependent functions of RSK2 and the apoptosis-promoting factor TIA-1 in stress granule assembly and cell survival.
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DOI：
10.1016/j.molcel.2008.06.025
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发表时间：
2008-09-05
期刊：
影响因子：
16
通讯作者：
Lannigan, Deborah A.
中科院分区：
文献类型：
--
作者：
Eisinger-Mathason, T. S. Karin;Andrade, Josefa;Groehler, Angela L.;Clark, David E.;Muratore-Schroeder, Tara L.;Pasic, Lejla;Smith, Jeffrey A.;Shabanowitz, Jeffrey;Hunt, Donald F.;Macara, Ian G.;Lannigan, Deborah A.
应激颗粒通过作为翻译抑制位点来帮助细胞在环境应激条件下存活。我们报告了应激颗粒与丝氨酸/苏氨酸激酶RSK2之间的意想不到的联系。在应激的乳腺细胞中，内源性RSK2与TIA-1和多-(A)结合蛋白1在颗粒中共定位，RSK2和TIA-1的分离表现出共依赖性。RSK2 n端激酶结构域控制TIA-1与朊病毒相关结构域的直接相互作用。沉默RSK2会降低细胞对应激反应的存活率。丝裂原从应激颗粒中释放RSK2，并通过c端核细胞质穿梭序列进入细胞核。核积累依赖于TIA-1。令人惊讶的是，在没有其他活性信号通路的情况下，RSK2的核定位足以通过诱导细胞周期蛋白D1来增强增殖。因此，RSK2是连接应激反应与存活和增殖的关键因子。
Stress granules aid cell survival in response to environmental stressors by acting as sites of translational repression. We report an unanticipated link between stress granules and the Ser/Thr kinase, RSK2. In stressed breast cells endogenous RSK2 co-localizes in granules with TIA-1 and poly-(A) binding protein 1, and the sequestration of RSK2 and TIA-1 exhibits co-dependency. The RSK2 N-terminal kinase domain controls the direct interaction with the prion-related domain of TIA-1. Silencing RSK2 decreases cell survival in response to stress. Mitogen releases RSK2 from the stress granules and permits its nuclear import via a nucleo-cytoplasmic shuttling sequence in the C-terminal domain. Nuclear accumulation is dependent on TIA-1. Surprisingly, nuclear localization of RSK2 is sufficient to enhance proliferation through induction of cyclin D1, in the absence of other active signaling pathways. Hence, RSK2 is a pivotal factor linking the stress response to survival and proliferation.
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影响因子：
5.3
作者：
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通讯作者：
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影响因子：
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DOI：
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DOI：
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发表时间：
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影响因子：
11.1
作者：
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影响因子：
3.3
作者：
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