The Nm23-H1-h-Prune complex in cellular physiology: a 'tip of the iceberg' protein network perspective
The Nm23-H1-h-Prune complex in cellular physiology: a 'tip of the iceberg' protein network perspective
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DOI：
10.1007/s11010-009-0115-4
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发表时间：
2009-09-01
影响因子：
4.3
通讯作者：
Zollo, Massimo
中科院分区：
文献类型：
--
作者：
Galasso, Alessia;Zollo, Massimo
Nm 23-H1（也称为NDPKA）和h-Prune形成一种蛋白质复合物，是一种鲜为人知的蛋白质网络的一部分。该复合物的修饰与癌症状态相关。在这里，我们专注于Nm 23-H1-H-Prune复合物在细胞生理学中的作用，通过分析Nm 23-H1和H-Prune的“结合”和“非结合”状态之间的平衡，从而我们推测在非平衡条件下细胞稳态期间的“读出”。我们已经分析了Nm 23-H1和h-Prune单独和组合的生物化学活性，重点是Nm 23-H1的抗转移活性。然后，我们研究了负责Nm 23-H1-h-Prune复合物形成的细胞机制。为了评估Nm 23-H1-h-Prune复合物的形成与Nm 23-H1和h-Prune的“游离”水平之间的平衡的重要性，我们提出了一种基于促癌条件的模型，其中这种平衡受到负面影响。
Nm23-H1 (also known as NDPKA) and h-Prune form a protein complex that is part of a little-understood protein network. Modifications of this complex correlate with cancer status. Here, we focus on the role of the Nm23-H1-h-Prune complex in cellular physiology, through an analysis of the balance between the 'bound' and 'non-bound' states of Nm23-H1 and h-Prune, whereby we speculate on the 'read-out' during cell homeostasis under non-balanced conditions. We have analysed the biochemical activities of both Nm23-H1 and h-Prune alone and in combination, focussing on the anti-metastatic activity of Nm23-H1. We have then investigated the cellular mechanisms responsible for the formation of the Nm23-H1-h-Prune complex. To evaluate the importance of the equilibrium between the formation of the Nm23-H1-h-Prune complex and the 'free' levels of Nm23-H1 and h-Prune, we propose a model based on a pro-cancer condition where this equilibrium is negatively affected.