In mammals, virtually all body cells harbor cell-autonomous and self-sustained circadian oscillators that rely on delayed negative feedback loops in gene expression. Transcriptional activation and repression play a major role in keeping these clocks ticking, but numerous post-translational mechanisms—and particularly the phosphorylation of core clock components by protein kinases—are also critically involved in setting the pace of these timekeepers. In this issue of Genes & Development, Klemz and colleagues (pp. 1161–1174) now show how dephosphorylation of BMAL1 by protein phosphatase 4 (PPP4) participates in the modulation of circadian timing.

中文翻译：

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BMAL1去磷酸化决定了生物钟的节奏

在哺乳动物中，几乎所有的身体细胞都具有细胞自主和自我维持的昼夜节律振荡器，其依赖于基因表达中延迟的负反馈回路。转录激活和抑制在保持这些时钟滴答作响方面发挥着重要作用，但许多翻译后机制——尤其是蛋白激酶对核心时钟成分的磷酸化——也与设定这些计时员的节奏密切相关。在本期《基因与发展》中，Klemz 及其同事 (pp. 1161–1174) 现在展示了蛋白磷酸酶 4 (PPP4) 对 BMAL1 的去磷酸化如何参与调节昼夜节律。