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首页> 外文期刊>Cell metabolism >Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1
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Acetylation negatively regulates glycogen phosphorylase by recruiting protein phosphatase 1

机译：乙酰化通过募集蛋白磷酸酶1负调节糖原磷酸化酶

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摘要

Glycogen phosphorylase (GP) catalyzes the rate-limiting step in glycogen catabolism and plays a key role in maintaining cellular and organismal glucose homeostasis. GP is the first protein whose function was discovered to be regulated by reversible protein phosphorylation, which is controlled by phosphorylase kinase (PhK) and protein phosphatase 1 (PP1). Here we report that lysine acetylation negatively regulates GP activity by both inhibiting enzyme activity directly and promoting dephosphorylation. Acetylation of GP Lys 470 enhances its interaction with the PP1 substrate-targeting subunit, G L, and PP1, thereby promoting GP dephosphorylation and inactivation. We show that GP acetylation is stimulated by glucose and insulin and inhibited by glucagon. Our results provide molecular insights into the intricate regulation of the classical GP and a functional crosstalk between protein acetylation and phosphorylation.
机译：糖原磷酸化酶（GP）催化糖原分解代谢中的限速步骤，在维持细胞和机体葡萄糖体内稳态中起关键作用。 GP是第一个发现其功能受可逆蛋白质磷酸化调节的蛋白质，该蛋白质受磷酸化酶激酶（PhK）和蛋白质磷酸酶1（PP1）控制。在这里我们报告说，赖氨酸乙酰化通过直接抑制酶活性和促进去磷酸化来负调节GP活性。 GP Lys 470的乙酰化可增强其与靶向PP1底物的亚基G L和PP1的相互作用，从而促进GP的去磷酸化和失活。我们显示GP乙酰化受到葡萄糖和胰岛素的刺激，并被胰高血糖素抑制。我们的结果为经典GP的复杂调节以及蛋白质乙酰化和磷酸化之间的功能性串扰提供了分子见解。

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