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Updated: Jun 23, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
Published on: October 15, 2019
The Nm23-H1-h-Prune complex in cellular physiology: a 'tip of the iceberg' protein network perspective
Alessia Galasso1, Massimo Zollo
1Centro di Ingegneria Genetica e Biotecnologia Avanzate (CEINGE), Via Comunale Margherita 482, 80145 Naples, Italy.
Abstract:
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.
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