![]() ![]() SUMOylation plays an important role in the scaffold function of PML. PML is not only responsible for maintaining the integrity of the complex but also for the recruitment and correct localization of all PML-NB proteins, e.g. The RBCC motif of the PML protein makes it possible to sustain a highly dynamic turnover of partner proteins during the cell cycle which could explain the functionally promiscuous nature of the PML-NBs. When correctly positioned, the coiled-coil domain is responsible for homo and hetero-dimer interactions between TRIM proteins. The B-box provides the correct orientation and alignment of the coiled-coil domain. This structure is ideal for the formation of larger protein aggregates and therefore crucial in processes such as cell growth, oncogenesis, apoptosis, and RNA trafficking during viral infections. The RING domain is a cysteine rich domain with zinc bound in a cross-brace conformation. It is characterized by an RBCC motif composed of a conserved RING domain, one or two B-boxes, and an α-helical coiled-coil domain. At the conserved N-terminus, PML contains a motif that defines the TRIM (Tripartite Motif) family of proteins. However, of these seven isoforms there are several alternative spliced variants yielding at least 18 different forms of PML. The PML gene consists of nine exons and alternative splicing yields six nuclear PML isoforms (PML I-VI) and one smaller cytoplasmatic isoform (PMLVII). ![]() These punctuate structures are now dubbed “PML nuclear bodies” (PML-NBs) after their scaffold protein Promyelocytic Leukaemia Protein (PML, also known as TRIM19 or MYL). Nuclear domain 10 (also called Kremer bodies or PODs) was first observed almost 50 years ago by electron microscopy as nuclear dense granular bodies. Keywords: PML-NB, SUMOylation, Cytoscape, protein-protein interaction, network Introduction Therefore, based on the PML network, we hypothesize that PML-NBs may function as a nuclear SUMOylation hotspot. Additionally, we show an enrichment of SUMOylatable proteins in the PML-NBs through an in-house prediction algorithm. By compiling 'the PML-ome', we highlighted the presence of interactors in the Small Ubiquitin Like Modifier (SUMO) conjugation pathway. Here we present a manually curated network of the PML-NB interactome based on extensive literature review including database information. To gain insight in PML-NB function, reductionist and high throughput techniques have been employed to identify PML-NB proteins. Promyelocytic Leukaemia Protein nuclear bodies (PML-NBs) are dynamic nuclear protein aggregates. Select the file that you have just downloaded and select import option Reference Manager (RIS). Available fromĬlick on Go to download the file. A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics. Van Damme E, Laukens K, Dang TH, Van Ostade X. ![]()
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