激酶 IKKi 使 GSK3α 酶失活,从而促进 AKT-mTOR 信号通路,介导白细胞介素-1 诱导的 Th17 细胞维持。

Inactivation of the enzyme GSK3α by the kinase IKKi promotes AKT-mTOR signaling pathway that mediates interleukin-1-induced Th17 cell maintenance.

机构信息

Department of Immunology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH 44195, USA.

出版信息

Immunity. 2012 Nov 16;37(5):800-12. doi: 10.1016/j.immuni.2012.08.019. Epub 2012 Nov 8.

Abstract

Interleukin-1 (IL-1)-induced activation of the mTOR kinase pathway has major influences on Th17 cell survival, proliferation, and effector function. Via biochemical and genetic approaches, the kinases IKKi and GSK3α were identified as the critical intermediate signaling components for IL-1-induced AKT activation, which in turn activated mTOR. Although insulin-induced AKT activation is known to phosphorylate and inactivate GSK3α and GSK3β, we found that GSK3α but not GSK3β formed a constitutive complex to phosphorylate and suppress AKT activation, showing that a reverse action from GSK to AKT can take place. Upon IL-1 stimulation, IKKi was activated to mediate GSK3α phosphorylation at S21, thereby inactivating GSK3α to promote IL-1-induced AKT-mTOR activation. Thus, IKKi has a critical role in Th17 cell maintenance and/or proliferation through the GSK-AKT-mTOR pathway, implicating the potential of IKKi as a therapeutic target.

摘要

白细胞介素-1(IL-1)诱导的 mTOR 激酶途径的激活对 Th17 细胞的存活、增殖和效应功能有重要影响。通过生化和遗传方法,鉴定出激酶 IKKi 和 GSK3α 是 IL-1 诱导的 AKT 激活的关键中间信号成分,而 AKT 又激活了 mTOR。虽然胰岛素诱导的 AKT 激活已知会磷酸化并失活 GSK3α 和 GSK3β,但我们发现 GSK3α 而不是 GSK3β 形成一个组成性复合物来磷酸化并抑制 AKT 激活,表明 GSK 对 AKT 可以发生逆向作用。在 IL-1 刺激下,IKKi 被激活以介导 GSK3α 在 S21 的磷酸化,从而使 GSK3α 失活,促进 IL-1 诱导的 AKT-mTOR 激活。因此,IKKi 通过 GSK-AKT-mTOR 途径在 Th17 细胞的维持和/或增殖中起着关键作用,这暗示了 IKKi 作为治疗靶点的潜力。

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