The Nucleolus

Pederson, Thoru

doi:10.1101/cshperspect.a000638

Cited by 360 publications

(289 citation statements)

References 87 publications

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“…To see this illustration in color, the reader is referred to the web version of this article at www.liebertpub.com/ars 624 ANTONIALI ET AL. (114,115). The ability of different proteins to localize within the nucleolus has been linked to the stable interaction with anchored resident proteins, such as NPM1 or nucleolin (NCL), that may act as carriers, or as a retention scaffolds, supporting the idea that the residence time of proteins within the nucleolar compartment is strongly related to their specific interactions in a process known as ''nucleolar sequestration'' (40,115,130).…”

Section: The Way To Move: Visitors Versus Resident Nucleolar Proteinsmentioning

confidence: 92%

“…Ribosomal structural proteins are imported from the cytoplasm in supra-stoichiometric complexes and exported in the form of assembled ribosomal subunits; this ensures that RPs are never rate-limiting for the ribosomal assembly (83). The excess of protein undergoes ubiquitylation and degradation in the nucleoplasm through the proteasome system (114,129), indicating that mammalian cells produce large amount of these proteins and degrade those that are not assembled with rRNA. district.…”

Section: Structure Composition and Classical Functions Of The Nuclementioning

confidence: 99%

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Emerging Roles of the Nucleolus in Regulating the DNA Damage Response: The Noncanonical DNA Repair Enzyme APE1/Ref-1 as a Paradigmatical Example

Antoniali

Lirussi

Poletto

et al. 2014

Antioxidants & Redox Signaling

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Significance: An emerging concept in DNA repair mechanisms is the evidence that some key enzymes, besides their role in the maintenance of genome stability, display also unexpected noncanonical functions associated with RNA metabolism in specific subcellular districts (e.g., nucleoli). During the evolution of these key enzymes, the acquisition of unfolded domains significantly amplified the possibility to interact with different partners and substrates, possibly explaining their phylogenetic gain of functions. Recent Advances: After nucleolar stress or DNA damage, many DNA repair proteins can freely relocalize from nucleoli to the nucleoplasm. This process may represent a surveillance mechanism to monitor the synthesis and correct assembly of ribosomal units affecting cell cycle progression or inducing p53-mediated apoptosis or senescence. Critical Issues: A paradigm for this kind of regulation is represented by some enzymes of the DNA base excision repair (BER) pathway, such as apurinic/apyrimidinic endonuclease 1 (APE1). In this review, the role of the nucleolus and the noncanonical functions of the APE1 protein are discussed in light of their possible implications in human pathologies. Future Directions: A productive cross-talk between DNA repair enzymes and proteins involved in RNA metabolism seems reasonable as the nucleolus is emerging as a dynamic functional hub that coordinates cell growth arrest and DNA repair mechanisms. These findings will drive further analyses on other BER proteins and might imply that nucleic acid processing enzymes are more versatile than originally thought having evolved DNA-targeted functions after a previous life in the early RNA world. Antioxid. Redox Signal. 20, 621-639.

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Section: The Way To Move: Visitors Versus Resident Nucleolar Proteinsmentioning

confidence: 92%

Section: Structure Composition and Classical Functions Of The Nuclementioning

confidence: 99%

Emerging Roles of the Nucleolus in Regulating the DNA Damage Response: The Noncanonical DNA Repair Enzyme APE1/Ref-1 as a Paradigmatical Example

Antoniali

Lirussi

Poletto

et al. 2014

Antioxidants & Redox Signaling

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“…Electromicrographic studies have shown that nucleoli contain several distinct substructures, with the number and nature of these structures differing between species; anamniotic eukaryotes and the evolutionarily ancient turtles show a bipartite nucleolus, containing Fibrillar (F) and Granular (G) Zones, while the remaining amniotes exhibit a tripartite nucleolus containing a distinct Fibrillar Centre (FC), Dense Fibrillar Component (DFC) and Granular Component (GC; Lamaye et al 2011;Thiry and Lafontaine 2005). Since the mid-1960s the nucleolus has been known as the site of ribosomal RNA (rRNA) transcription, processing and ribosomal assembly, and the different substructures within the nucleolus likely mediate distinct stages of the ribosome assembly process (Pederson 2011;Hernandez-Verdun et al 2010). Several decades of research by many groups have made great strides towards elucidating the complicated succession of processing steps required to assemble nascent rRNA into functional ribosomes, as well as the identifying the ~80 ribosomal proteins (RPs) and >300 ribosomal maturation factors that are required to accomplish them (Henras et al 2014;Venema and Tollervey, 1999;Woolford and Baserga 2013).…”

Section: Introductionmentioning

confidence: 99%

Nucleolin and nucleophosmin: nucleolar proteins with multiple functions in DNA repair

Scott

Oeffinger

2016

Biochem. Cell Biol.

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The nucleolus represents a highly multifunctional intranuclear organelle in which, in addition to the canonical ribosome assembly, numerous processes such as transcription, DNA repair and replication, the cell cycle and apoptosis are coordinated. The nucleolus is further a key hub in the sensing of cellular stress and undergoes major structural and compositional changes in response to cellular perturbations.Numerous nucleolar proteins have been identified that, upon nucleolar stress sensing, deploy additional, non-ribosomal roles in the regulation of varied cell processes including cell cycle arrest, arrest of DNA replication, induction of DNA repair, and apoptosis, among others. The highly abundant proteins nucleophosmin (NPM1) and nucleolin (NCL) are two such factors that transit to the nucleoplasm in response to stress, and participate directly in the repair of numerous different DNA damages. This review discusses the contributions made by NCL and/or NPM1 to the different DNA repair pathways employed by mammalian cells to repair DNA insults, and examines the implications of such activities for the regulation, pathogenesis and therapeutic targeting of NPM1 and NCL.

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“…In comparison to the visible light micrograph (Fig. 6.2a) the globular dense regions (indicated by the black arrows) can be assigned to nucleoli [204,205]. Note that additional strongly scattering material, which we assign to heterochromatin, is not visible in the visible light micrograph.…”

Section: ) X-ray Dark-field Image Of the Roi Indicated In A) The Scamentioning

confidence: 99%

Investigating Cellular Nanoscale with X-rays

Hémonnot¹

2016

Göttingen Series in X-Ray Physics

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The Nucleolus

Cited by 360 publications

References 87 publications

Emerging Roles of the Nucleolus in Regulating the DNA Damage Response: The Noncanonical DNA Repair Enzyme APE1/Ref-1 as a Paradigmatical Example

Emerging Roles of the Nucleolus in Regulating the DNA Damage Response: The Noncanonical DNA Repair Enzyme APE1/Ref-1 as a Paradigmatical Example

Nucleolin and nucleophosmin: nucleolar proteins with multiple functions in DNA repair

Investigating Cellular Nanoscale with X-rays

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