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

Int J Biol Sci

Laboratory of Protein Chemistry, Proteomics and Signal Transduction, Department of Biomedical Sciences, University of Antwerp (Campus Drie Eiken), Universiteitsplein 1 - Building T, Wilrijk, Belgium.

Published: January 2010

AI Article Synopsis

  • PML-NBs are dynamic nuclear aggregates that play a crucial role in cellular functions, and the study aims to better understand their interactions.
  • A comprehensive network, called 'the PML-ome', has been created by reviewing existing literature to identify proteins associated with PML-NBs.
  • The research suggests that PML-NBs could act as a central site for SUMOylation, based on the presence of SUMO pathway interactors and a prediction model highlighting SUMOylatable proteins within these nuclear bodies.

Article 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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2808052PMC
http://dx.doi.org/10.7150/ijbs.6.51DOI Listing

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