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ISSN 1449-2288 |
Int J Biol Sci 2010; 6:51-67 ©Ivyspring International Publisher Review A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics 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. 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 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; 6:51-67. Available from http://www.biolsci.org/v06p0051.htm |