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Int J Biol Sci 2010; 6(1):51-67. doi:10.7150/ijbs.6.51

Review

A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics

Ellen Van Damme1, Kris Laukens2, Thanh Hai Dang2, Xaveer Van Ostade1 ✉

1. Laboratory of Protein Chemistry, Proteomics and Signal Transduction, Department of Biomedical Sciences, University of Antwerp (Campus Drie Eiken), Universiteitsplein 1 - Building T, 2610 Wilrijk, Belgium.
2. Intelligent Systems Laboratory (ISLab) Department of Mathematics and Computer Science, University of Antwerp (Campus Middelheim), Middelheimlaan 1 - Building G, 2020 Antwerp, Belgium

Abstract

Promyelocytic Leukaemia Protein nuclear bodies (PML-NBs) are dynamic nuclear protein aggregates. To gain insight in PML-NB function, reductionist and high throughput techniques have been employed to identify PML-NB proteins. Here we present a manually curated network of the PML-NB interactome based on extensive literature review including database information. By compiling 'the PML-ome', we highlighted the presence of interactors in the Small Ubiquitin Like Modifier (SUMO) conjugation pathway. Additionally, we show an enrichment of SUMOylatable proteins in the PML-NBs through an in-house prediction algorithm. Therefore, based on the PML network, we hypothesize that PML-NBs may function as a nuclear SUMOylation hotspot.

Keywords: PML-NB, SUMOylation, Cytoscape, protein-protein interaction, network

This is an open access article distributed under the terms of the Creative Commons Attribution (CC BY-NC) License. See http://ivyspring.com/terms for full terms and conditions.
How to cite this article:
Van Damme E, Laukens K, Dang TH, Van Ostade X. A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics. Int J Biol Sci 2010; 6(1):51-67. doi:10.7150/ijbs.6.51. Available from http://www.ijbs.com/v06p0051.htm