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调控蛋白质相互作用的关键酶

最新的研究发现了一种调控蛋白质相互作用的关键酶,PP1。研究发现,PP1会“选择”蛋白,这是一项很重要的发现,错误的PP1调控会引起许多疾病,包括癌症,糖尿病和帕金森氏病等。

这项研究成果发表在3月21日出版 Nature Structural & Molecular Biology 杂志网络版上。

参考文献:Nature Structural & Molecular Biology

Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites
Michael J Ragusa,Barbara Dancheck,David A Critton,Angus C Nairn,Rebecca Page& Wolfgang Peti
Affiliations Contributions Corresponding author Journal name:
Nature Structural & Molecular Biology
Year published: (2010) DOI: doi:10.1038/nsmb.1786
Received 09 December 2009 Accepted 08 February 2010 Published online 21 March 2010

Abstract

The serine/threonine protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets. PP1 associates with ≥200 regulatory proteins to form highly specific holoenzymes. These regulatory proteins target PP1 to its point of action within the cell and prime its enzymatic specificity for particular substrates. However, how they direct PP1's specificity is not understood. Here we show that spinophilin, a neuronal PP1 regulator, is entirely unstructured in its unbound form, and it binds PP1 through a folding-upon-binding mechanism in an elongated fashion, blocking one of PP1's three putative substrate binding sites without altering its active site. This mode of binding is sufficient for spinophilin to restrict PP1's activity toward a model substrate in vitro without affecting its ability to dephosphorylate its neuronal substrate, glutamate receptor 1 (GluR1). Thus, our work provides the molecular basis for the ability of spinophilin to dictate PP1 substrate specificity.

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    摘要
    最新的研究发现了一种调控蛋白质相互作用的关键酶,PP1。研究发现,PP1会“选择”蛋白,这是一项很重要的发现,错误的PP1调控会引起许多疾病,包括癌症,糖尿病和帕金森氏病等。
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