Literature DB >> 19390954

The Nm23-H1-h-Prune complex in cellular physiology: a 'tip of the iceberg' protein network perspective.

Alessia Galasso1, Massimo Zollo.   

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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Year:  2009        PMID: 19390954     DOI: 10.1007/s11010-009-0115-4

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  63 in total

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