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

Mol Cell Biochem. 2009 Sep;329(1-2):149-59. doi: 10.1007/s11010-009-0115-4. Epub 2009 Apr 24.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Physiological Phenomena*
  • Gene Expression Regulation, Neoplastic
  • Humans
  • NM23 Nucleoside Diphosphate Kinases / genetics
  • NM23 Nucleoside Diphosphate Kinases / metabolism*
  • Neoplasm Metastasis / genetics*
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism*
  • Neoplasms / genetics*
  • Phosphoric Monoester Hydrolases

Substances

  • Carrier Proteins
  • NM23 Nucleoside Diphosphate Kinases
  • Neoplasm Proteins
  • PRUNE1 protein, human
  • Phosphoric Monoester Hydrolases