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

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...

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Detalles Bibliográficos
Autores principales: Van Damme, Ellen, Laukens, Kris, Dang, Thanh Hai, Van Ostade, Xaveer
Formato: Texto
Lenguaje:English
Publicado: Ivyspring International Publisher 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2808052/
https://www.ncbi.nlm.nih.gov/pubmed/20087442
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author Van Damme, Ellen
Laukens, Kris
Dang, Thanh Hai
Van Ostade, Xaveer
author_facet Van Damme, Ellen
Laukens, Kris
Dang, Thanh Hai
Van Ostade, Xaveer
author_sort Van Damme, Ellen
collection PubMed
description 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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spelling pubmed-28080522010-01-19 A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics Van Damme, Ellen Laukens, Kris Dang, Thanh Hai Van Ostade, Xaveer Int J Biol Sci Review 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. Ivyspring International Publisher 2010-01-12 /pmc/articles/PMC2808052/ /pubmed/20087442 Text en © Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.
spellingShingle Review
Van Damme, Ellen
Laukens, Kris
Dang, Thanh Hai
Van Ostade, Xaveer
A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
title A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
title_full A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
title_fullStr A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
title_full_unstemmed A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
title_short A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
title_sort manually curated network of the pml nuclear body interactome reveals an important role for pml-nbs in sumoylation dynamics
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2808052/
https://www.ncbi.nlm.nih.gov/pubmed/20087442
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