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首页> 外文期刊>Journal of Molecular Biochemistry >Cell cycle-dependent phosphorylation of nucleophosmin and its potential regulation by peptidyl-prolyl cis/trans isomerase
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Cell cycle-dependent phosphorylation of nucleophosmin and its potential regulation by peptidyl-prolyl cis/trans isomerase

机译：核磷蛋白的细胞周期依赖性磷酸化及其通过肽基脯氨酰顺/反异构酶的潜在调控

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摘要

Nucleophosmin (NPM) is a ubiquitously expressed phosphoprotein involved in many cellular processes. Phosphorylation is considered the major regulatory mechanism of the NPM protein, associated with diverse cellular events. In this study, we characterized the phosphorylation status of several physiological phosphorylation sites of NPM, especially the newly confirmed in vivo site threonine 95 (Thr95). NPM-Thr95 exhibits a transient and cell cycle-dependent phosphorylation state compared to several other in vivo phosphorylation sites examined, including Ser4, Thr199 and Thr234/Thr237. In addition, we characterized a functional interaction between NPM and the peptidyl-prolyl isomerase Pin1, which specifically bind to each other during mitosis. The demonstration of this binding represents a novel post-phosphorylation regulatory mechanism for NPM that has not been investigated before. Mutated Pin1 putative binding sites result in defected cell division and reduced number of mitotic cells, suggesting that post-phosphorylation is important for NPM in regulating cell cycle progression.
机译：核蛋白（NPM）是一种普遍表达的磷蛋白，参与许多细胞过程。磷酸化被认为是NPM蛋白的主要调控机制，与多种细胞事件有关。在这项研究中，我们表征了NPM的几个生理磷酸化位点的磷酸化状态，尤其是新近证实的体内苏氨酸95（Thr95）。与所检查的其他几个体内磷酸化位点（包括Ser4，Thr199和Thr234 / Thr237）相比，NPM-Thr95表现出瞬时的且依赖细胞周期的磷酸化状态。此外，我们表征了NPM和肽基-脯氨酰异构酶Pin1之间的功能相互作用，它们在有丝分裂过程中彼此特异性结合。这种结合的证明代表了以前从未研究过的NPM的新型磷酸化后调控机制。突变的Pin1推定的结合位点导致缺陷的细胞分裂和有丝分裂细胞的数量减少，这表明磷酸化后对于NPM在调节细胞周期进程中很重要。

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