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Rapamycin inhibition of baculovirus recombinant (BVr) ribosomal protein S6 kinase (S6K1) is mediated by an event other than phosphorylation

机译:雷帕霉素对杆状病毒重组(BVr)核糖体蛋白S6激酶(S6K1)的抑制作用是由磷酸化以外的事件介导的

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摘要

BackgroundRibosomal protein S6 kinase 1(S6K1) is an evolutionary conserved kinase that is activated in response to growth factors and viral stimuli to influence cellular growth and proliferation. This downstream effector of target of rapamycin (TOR) signaling cascade is known to be directly activated by TOR- kinase mediated hydrophobic motif (HM) phosphorylation at Threonine 412 (T412). Selective loss of this phosphorylation by inactivation of TOR kinase or activation/recruitment of a phosphatase has accordingly been implicated in mediating inhibition by rapamycin.
机译:背景核糖体蛋白S6激酶1(S6K1)是一种进化保守的激酶,可响应生长因子和病毒刺激而激活,从而影响细胞的生长和增殖。已知雷帕霉素(TOR)信号级联靶标的下游效应物可被苏氨酸412(T412)上的TOR激酶介导的疏水基序(HM)磷酸化直接激活。因此,已经通过TOR激酶的失活或磷酸酶的激活/招募选择性丧失了这种磷酸化作用,这与雷帕霉素介导的抑制作用有关。

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