PML nuclear bodies: from architecture to function

Lallemand-Breitenbach, Valérie; Thé, Hugues de

doi:10.1016/j.ceb.2018.03.011

Cited by 199 publications

(190 citation statements)

References 73 publications

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“…PML bodies host more than 150 proteins with a wide range of functions, such as DNA repair, stress response, senescence, antiviral immunity, and tumor suppression (Sahin et al, 2014). These proteins appear to carry out some of their roles within PML bodies, though a unifying model for PML body functions remain to be established (Lallemand-Breitenbach and de The, 2018). It was noted early on that PML proteins and many other PML body constituents are sumoylated and contain SIMs; importantly, mutations affecting their sumoylation or SIMs were shown to impair PML body formation or constituent recruitment (Sahin et al, 2014; Shen et al, 2006).…”

Section: Sumo Affects Nuclear Structures and Functionsmentioning

confidence: 99%

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

2018

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Summary Since the discovery of SUMO twenty years ago, SUMO conjugation has become a widely-recognized post-translational modification that targets a myriad of proteins in many processes. Great progress has been made in understanding the SUMO pathway enzymes, substrate sumoylation, and the interplay between sumoylation and other regulatory mechanisms in a variety of contexts. As these research directions continue to generate insights into SUMO-based regulation, several mechanisms by which sumoylation and desumoylation can orchestrate large biological effects are emerging. These include the ability to target multiple proteins within the same cellular structure or process, respond dynamically to external and internal stimuli, and modulate signaling pathways involving other post-translational modifications. Focusing on nuclear function and intracellular signaling, this review highlights a broad spectrum of historical data and recent advances with the aim of providing an overview of mechanisms underlying SUMO-mediated global effects to stimulate further inquiry into intriguing roles of SUMO.

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Section: Sumo Affects Nuclear Structures and Functionsmentioning

confidence: 99%

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

2018

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“…These PML nuclear body‐enriched proteins are often ligated to small ubiquitin‐like modifier (SUMO), which aids the recruitment of other proteins to the body and a high number of reported binary interactions (Table , Matunis, Zhang, & Ellis, ). Key PML nuclear body functions include the response to oxidative stress, viral infection, chromatin remodeling, and transcription (Lallemand‐Breitenbach & de Thé, ). These are achieved by SUMOylation of effector molecules by the SUMO E2 ligase UBC9, which directly interacts with PML and is dependent upon PML tetramerization for recruitment via the RING domain (Wang et al, ).…”

Section: Various Nuclear Bodies Exhibit Rna‐related Functional Architmentioning

confidence: 99%

Membraneless nuclear organelles and the search for phases within phases

2018

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Cells are segregated into two distinct compartment groups to optimize cellular function. The first is characterized by lipid membranes that encapsulate specific regions and regulate macromolecular flux. The second, known collectively as membraneless organelles (MLOs), lacks defining lipid membranes and exhibits self‐organizing properties. MLOs are enriched with specific RNAs and proteins that catalyze essential cellular processes. A prominent sub‐class of MLOs are known as nuclear bodies, which includes nucleoli, paraspeckles, and other droplets. These microenvironments contain specific RNAs, exhibit archetypal liquid–liquid phase separation characteristics, and harbor intrinsically disordered, multivalent hub proteins. We present an analysis of nuclear body protein disorder that suggests MLO proteomes are significantly more disordered than structured cellular features. We also outline common MLO ultrastructural features, exemplified by the three sub‐compartments present inside the nucleolus. A core‐shell configuration, or phase within a phase, is displayed by several nuclear bodies and may be functionally important. Finally, we summarize evidence indicating extensive RNA and protein sharing between distinct nuclear bodies, suggesting functional cooperation and similar nucleation principles. Considering the substantial accumulation of specific coding and noncoding RNA classes inside MLOs, evidence that RNA buffers specific phase transition events, and the absence of a clear correlation between total intrinsic protein disorder and MLO accumulation, we conclude that RNA biogenesis may play a key role in MLO formation, internal organization, and function. This article is categorized under: RNA Export and Localization > RNA Localization RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications

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“…PML-NB are multiprotein complexes that exhibit a discreet, punctate appearance in the nucleus of a cell [57,58]. PML-NB have been implicated in a number of cellular processes including transcriptional regulation, the regulation of apoptosis, DNA damage repair, protein modification, and antiviral responses [64]. The reorganization of PML-NB by E4-ORF3 requires higher-order multimerization by this viral protein [59,60].…”

Section: E4-orf3 and Regulation Of Innate Responsesmentioning

confidence: 99%

“…E4-ORF3 targets PML isoform II during the process of PML-NB disruption, and PML-II promotes the innate response to Ad infection [61][62][63]. PML-NB have been implicated in a number of cellular processes including transcriptional regulation, the regulation of apoptosis, DNA damage repair, protein modification, and antiviral responses [64]. PML-NB have also been shown to react to stresses, such as heat shock and heavy metals as well as IFN, suggesting a role in cellular defense mechanisms.…”

Section: E4-orf3 and Regulation Of Innate Responsesmentioning

confidence: 99%

Adenoviral strategies to overcome innate cellular responses to infection

Sohn

Hearing

2019

FEBS Letters

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Viruses alter host cell processes to optimize their replication cycle. Human adenoviruses (Ad) encode proteins that promote viral macromolecular synthesis and counteract innate and adaptive responses to infection. The focus of this review is on how Ad evades innate cellular responses to infection, including an interferon (IFN) response and a DNA damage response (DDR). Ad blocks the IFN response by inhibiting cytoplasmic signaling pathways and the activation of IFN-stimulated genes (ISGs), as well as the functions of ISG products, such as PML. Ad also inhibits DDR sensors, for instance, the Mre11-Rad50-Nbs1 complex, and DDR effectors like DNA ligase IV. These innate cellular responses impact many different viruses, and studies on Ad have provided broad insight into these areas.

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PML nuclear bodies: from architecture to function

Cited by 199 publications

References 73 publications

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes

Membraneless nuclear organelles and the search for phases within phases

Adenoviral strategies to overcome innate cellular responses to infection

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