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首页> 外文期刊>Science Advances >Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme
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Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme

机译：肌肉糖原蛋白磷酸酶1全酶的底物募集机制的鉴定

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Glycogen is the primary storage form of glucose. Glycogen synthesis and breakdown are tightly controlled by glycogen synthase (GYS) and phosphorylase, respectively. The enzyme responsible for dephosphorylating GYS and phosphorylase, which results in their activation (GYS) or inactivation (phosphorylase) to robustly stimulate glycogen synthesis, is protein phosphatase 1 (PP1). However, our understanding of how PP1 recruits these substrates is limited. Here, we show how PP1, together with its muscle glycogen–targeting (GM) regulatory subunit, recruits and selectively dephosphorylates its substrates. Our molecular data reveal that the GM carbohydrate binding module (GMCBM21), which is amino-terminal to the GM PP1 binding domain, has a dual function in directing PP1 substrate specificity: It either directly recruits substrates (i.e., GYS) or recruits them indirectly by localization (via glycogen for phosphorylase). Our data provide the molecular basis for PP1 regulation by GM and reveal how PP1-mediated dephosphorylation is driven by scaffolding-based substrate recruitment.
机译：糖原是葡萄糖的主要储存形式。糖原合成酶和分解分别由糖原合酶（GYS）和磷酸化酶严格控制。负责使GYS和磷酸化酶去磷酸化的酶是蛋白质磷酸酶1（PP1），该酶可导致它们的活化（GYS）或失活（磷酸化酶）以强烈刺激糖原合成。但是，我们对PP1如何募集这些底物的理解是有限的。在这里，我们展示了PP1及其肌肉靶向糖原（GM）调节亚基如何募集并选择性地使其底物去磷酸化。我们的分子数据表明，GM碳水化合物结合模块（GMCBM21）位于GM PP1结合域的氨基末端，在指导PP1底物特异性方面具有双重功能：它直接募集底物（即GYS）或间接募集底物。通过定位（通过糖原磷酸化酶）。我们的数据为GM调控PP1提供了分子基础，并揭示了基于脚手架的底物募集是如何驱动PP1介导的去磷酸化的。

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