Proteomic profiling of the human T-cell nucleolus

Jarboui, Mohamed Ali; Wynne, Kieran; Elia, Giuliano; Hall, William W.; Gautier, Virginie

doi:10.1016/j.molimm.2011.09.005

Cited by 47 publications

(84 citation statements)

References 124 publications

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“…Nucleoli are non-membrane-bound nuclear compartments, well described and analysed in details since the last millennium. 51,52 They are responsible for ribosome biogenesis and diverse cellular functions and processes such as cell cycle control, cellular stress response, nuclear export and sequestration of key proteins regulators of cell-cycle activity and response to apoptosis and early stage cellular response to toxic such as chemotherapeutic drugs. 30 The size, number and organisation of nucleoli are cell-specific and nuclear proteins, notably histone, play an important role in the nucleoli stability and functions.…”

Section: Pca-ldamentioning

confidence: 99%

Cellular discrimination using in vitro Raman micro spectroscopy: the role of the nucleolus

Farhane

Bonnier

Casey

et al. 2015

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Section: Pca-ldamentioning

confidence: 99%

Cellular discrimination using in vitro Raman micro spectroscopy: the role of the nucleolus

Farhane

Bonnier

Casey

et al. 2015

Analyst

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“…Some of the splice variants generate C-terminally extended protein isoforms referred to as NF110 (NFAR-2) (24, 25), which also interact with NF45 (26). Compared to NF90, NF110 displays a stronger association with chromatin and has been mainly linked to transcription (26-28).Interestingly, NF45 and NF90 have been identified as parts of the nucleolar proteome by mass spectrometric analysis (29,30). The biological significance of this potential nucleolar localization, however, has not been explored.…”

mentioning

confidence: 99%

“…Interestingly, NF45 and NF90 have been identified as parts of the nucleolar proteome by mass spectrometric analysis (29,30). The biological significance of this potential nucleolar localization, however, has not been explored.…”

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confidence: 99%

The NF45/NF90 Heterodimer Contributes to the Biogenesis of 60S Ribosomal Subunits and Influences Nucleolar Morphology

Wandrey

Montellese

Koós

et al. 2015

Molecular and Cellular Biology

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dThe interleukin enhancer binding factors ILF2 (NF45) and ILF3 (NF90/NF110) have been implicated in various cellular pathways, such as transcription, microRNA (miRNA) processing, DNA repair, and translation, in mammalian cells. Using tandem affinity purification, we identified human NF45 and NF90 as components of precursors to 60S (pre-60S) ribosomal subunits. NF45 and NF90 are enriched in nucleoli and cosediment with pre-60S ribosomal particles in density gradient analysis. We show that association of the NF45/NF90 heterodimer with pre-60S ribosomal particles requires the double-stranded RNA binding domains of NF90, while depletion of NF45 and NF90 by RNA interference leads to a defect in 60S biogenesis. Nucleoli of cells depleted of NF45 and NF90 have altered morphology and display a characteristic spherical shape. These effects are not due to impaired rRNA transcription or processing of the precursors to 28S rRNA. Consistent with a role of the NF45/NF90 heterodimer in nucleolar steps of 60S subunit biogenesis, downregulation of NF45 and NF90 leads to a p53 response, accompanied by induction of the cyclin-dependent kinase inhibitor p21/CIP1, which can be counteracted by depletion of RPL11. Together, these data indicate that NF45 and NF90 are novel higher-eukaryote-specific factors required for the maturation of 60S ribosomal subunits. T he nuclear factors NF45 and NF90 (NFAR-1, DRBP76, MPP4, and TCP80) were originally discovered as a heterodimeric complex binding to the interleukin-2 (IL-2) promoter (1, 2) and are also referred to as interleukin enhancer-binding factors 2 (ILF2) and 3 (ILF3), respectively (3). While NF90 is vertebrate specific, NF45 is found throughout metazoans.In mammals, the NF45/NF90 complex is widely expressed across tissues (4). Over recent years, NF45/NF90 has been implicated in a great variety of biological processes. Apart from regulation of transcription (5-7), the heterodimer has also been linked to numerous other pathways, such as DNA damage response (8, 9), mRNA metabolism (10, 11), microRNA (miRNA) biogenesis (12), and viral infection (13-17). NF90 knockout mice display severe defects in skeletal muscle formation leading to respiratory failure soon after birth (18), indicating an essential role of NF90 function in vertebrate development.Both NF45 and NF90 possess an N-terminal "domain associated with zinc fingers" (DZF) that is found only in metazoan proteins. Recent structural analysis revealed that the DZF domains of NF45 and NF90 resemble template-free nucleotidyltransferases and mediate their heterodimerization through a structurally conserved interface (19). In addition to the DZF domain, NF90 possesses two double-stranded RNA binding domains (dsRBDs) in the C-terminal region (2, 20) that confer binding to highly structured RNAs (21-23).NF90 is expressed from at least five alternatively spliced mRNAs that all encode the DZF and dsRBDs. Some of the splice variants generate C-terminally extended protein isoforms referred to as NF110 (NFAR-2) (24, 25), which also interact with ...

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“…Furthermore, WDR43 copurifies with members of the human t-UTP/UTPA subcomplex (Freed et al 2012), highlighting its conserved evolutionary role. In humans and in zebrafish, WDR43 is a nucleolar protein like Utp5 in yeast (Ahmad et al 2009;Jarboui et al 2011;Zhao et al 2014). WDR43 localizes to all 3 subcompartments of nucleoli in HeLa cells by immunofluorescence (Wada et al 2014) and directly interacts with human UTP15 (hUTP15) and human UTP4/Cirhin (hUTP4/Cirhin) when reconstituted in vitro (Sato et al 2013).…”

Section: Role and Conservation Of Utp5/ Wdr43 In Other Eukaryotesmentioning

confidence: 99%

The Contributions of the Ribosome Biogenesis Protein Utp5/WDR43 to Craniofacial Development

2016

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Fairly recently, it was recognized that human ribosomopathies-developmental defects caused by mutations in ribosome biogenesis proteins-can exhibit tissue-specific defects rather than the expected global defects. This apparent anomaly-that seemingly ubiquitously expressed and required ribosomal proteins can have distinct functions in cell and tissue differentiation-has spurred new areas of research focused on better understanding translational mechanisms, biogenesis, and function in diverse cell types. This renewed appreciation for, and need to better understand, roles for ribosomal proteins in human development and disease has identified surprising similarities and differences in a variety of human ribosomopathies. Here, we discuss ribosomal protein functions in health and disease, focusing on the ribosome biogenesis protein Utp5/WDR43. New and exciting research in this field is anticipated to provide insight into a variety of previously understudied craniofacial dysostoses and result in significantly improved knowledge and understanding of roles for translational machinery in human craniofacial development and disease.

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Proteomic profiling of the human T-cell nucleolus

Cited by 47 publications

References 124 publications

Cellular discrimination using in vitro Raman micro spectroscopy: the role of the nucleolus

Cellular discrimination using in vitro Raman micro spectroscopy: the role of the nucleolus

The NF45/NF90 Heterodimer Contributes to the Biogenesis of 60S Ribosomal Subunits and Influences Nucleolar Morphology

The Contributions of the Ribosome Biogenesis Protein Utp5/WDR43 to Craniofacial Development

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