Nucleolar protein Nop25 is involved in nucleolar architecture

Suzuki, Shunji; Fujiwara, Takashi; Kanno, Motoko

doi:10.1016/j.bbrc.2007.05.069

Cited by 12 publications

(13 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mouse NOL12 localises to nucleoli in COS7 cells, and knocking down NOL12 function in this cell line results in nucleolar fragmentation (Suzuki et al, 2007). In budding yeast, the Nol12 homologue Rrp17p/Ydr412p has been implicated in nucleolar non-coding RNA processing events (Peng et al, 2003;Li et al, 2009;Oeffinger et al, 2009).…”

Section: Research Articlementioning

confidence: 99%

The Drosophila Nol12 homologue viriato is a dMyc target that regulates nucleolar architecture and is required for dMyc-stimulated cell growth

2011

View full text Add to dashboard Cite

SUMMARYThe nucleolus is a subnuclear factory, the activity of which is required beyond ribosome biogenesis for the regulation of cell growth, death and proliferation. In both Drosophila and mammalian cells, the activity of the nucleolus is regulated by the protooncogene Myc. Myc induces the transcription of genes required for ribosome biogenesis and the synthesis of rRNA by RNA polymerase I, a nucleolar event that is rate limiting for cell growth. Here, we show that the fruit fly Nol12 homologue Viriato is a key determinant of nucleolar architecture that is required for tissue growth and cell survival during Drosophila development. We further show that viriato expression is controlled by Drosophila Myc (dMyc), and that the ability of dMyc to stimulate nucleolar and cellular growth depends on viriato expression. Therefore, viriato acts downstream of dMyc to ensure a coordinated nucleolar response to dMyc-induced growth and, thereby, normal organ development. KEY WORDS: Drosophila, Cell proliferation, Cell growth, dMyc (Diminutive), Viriato, Nol12The Drosophila Nol12 homologue viriato is a dMyc target that regulates nucleolar architecture and is required for dMyc-stimulated cell growth HumanNOL12-GFP constructs were verified by DNA sequencing. Transgenic lines were generated by standard germline transformation methods and four independent lines were analysed. The Ubi-Gal4 driver was used to drive low-level expression of Vito-GFP in salivary glands, and ey-Gal4 was used to drive hNOL12-GFP expression during eye development and in salivary glands. ey-Gal4 drives 'leaky' Gal4 expression in the salivary glands. Mitotic recombinationMitotic recombination was induced using the Flp/FRT method. vito knockdown clones, or clones overexpressing dMyc alone or together with vitoRNAi, were induced by heat shock (1 hour at 37°C) at 48 ± 4 hours after egg laying (AEL) and dissected at 118 ± 4 hours AEL in larvae of the genotype y w hsflp/+; act>y+>Gal4, UAS-GFP/UAS-vitoRNAi, y w hsflp/+; act>y+>Gal4, UAS-GFP/+; UAS-dMyc/+ and y w hsflp/+; act>y+>Gal4, UAS-GFP/UAS-vitoRNAi; UAS-dMyc/+. ImmunostainingEye-antennal imaginal discs were prepared for immunohistochemistry using standard protocols. Primary antibodies used were: rabbit anti-cleaved Caspase-3 at 1:200 (Cell Signaling), mouse anti-Armadillo N27A1 at 1:100 [Developmental Studies Hybridoma Bank (DSHB)], mouse anti--galactosidase at 1:1000 (Promega, #Z3783), rat anti-Elav 7E8A10 at 1:100 (DSHB), mouse anti-Lamin ADL101 at 1:1 (DSHB), and rabbit antiFibrillarin at 1:250 (Abcam, #ab5821). Appropriate Alexa Fluorconjugated secondary antibodies were from Molecular Probes. Images were obtained with the Leica SP2 confocal system and processed with Adobe Photoshop. In situ hybridisationA digoxigenin (DIG)-labelled vito antisense RNA probe was synthesized by in vitro transcription with T7 RNA polymerase and DIG-UTP after linearisation of cDNA LD10447 with NotI and were used for whole-mount in situ hybridisation of fixed larvae. A sense RNA probe was used as a negative control. The DIG...

show abstract

Section: Research Articlementioning

confidence: 99%

The Drosophila Nol12 homologue viriato is a dMyc target that regulates nucleolar architecture and is required for dMyc-stimulated cell growth

2011

View full text Add to dashboard Cite

show abstract

“…Nucleolar morphology can be evaluated histologically using the toluidine blue staining. Numerous studies have reported that nucleolar fragmentation is part of the overall apoptotic morphology (Horky et al 2001;Fraschini et al 2005;Suzuki et al 2007). Here, we reported that oxidative stress (exposure to H 2 O 2 ) resulted into nucleolar segments (nucleolar fragmentation) in C 2 C 12 myogenic cells and MEFs.…”

Section: Discussionmentioning

confidence: 99%

“…Many evidences have suggested that the nucleolar segregation/fragmentation was induced by actinomycin D and adriamycin (Fraschini et al 2005), roscovitine (Wojciechowski et al 2003), cisplatin (Horky et al 2001), heat stress (Pelham 1984;Morcillo et al 1997) and UV irradiation (Al-Baker et al 2004). Evidence suggests that nucleolar segregation/fragmentation is a significant and early process during apoptosis (Horky et al 2001;Fraschini et al 2005;Suzuki et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Heat shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin

Wang

Deng

Chen

et al. 2012

Cell Stress and Chaperones

View full text Add to dashboard Cite

It has been reported that nucleolar fragmentation is a part of the overall apoptotic morphology, however, it is currently obscure whether and how nucleolar fragmentation can be induced by hydrogen peroxide (H 2 O 2 ) and heat shock protein 70 (Hsp70) can prevent nucleolar fragmentation. To dissect these two questions, C 2 C 12 myogenic cells and immortalized mouse embryonic fibroblasts (MEFs) with heat shock transcriptional factor 1 (HSF1) null mutation were treated with heat shock response (HS) (42.5±0.5°C for 1 h and recovery at 37°C for 24 h) and then were insulted with 0.5 mmol/L H 2 O 2 . Morphological changes of nucleoli were observed under contrast microscope or electronic microscope. It was found that (1) stimulation with H 2 O 2 -induced nucleolar fragmentation by mediating cleavage and down-regulation of nucleolar protein, nucleolin in C 2 C 12 myocytes and MEFs; (2) HS suppressed nucleolar fragmentation by inducing the expression of Hsp70 in an HSF1-dependent manner as indicated by assays of transfection with Hsp70 antisense oligonucleotides (AS-ONs) or recombinant plasmids of full-length Hsp70 cDNA; (3) protection of Hsp70 against nucleolar fragmentation was related to its accumulation in nucleolus mediated by nuclear localization sequence and its inhibition against cleavage and down-regulation of nucleolin. These results suggested that H 2 O 2 -induced nucleolar fragmentation and HS or Hsp70 inhibit H 2 O 2 -induced nucleolar fragmentation through the translocation of Hsp70 into nucleolar and its protection against impairment of nucleolin.

show abstract

“…45,46 siRNA to Nop25 caused nucleolar fragmentation. 47 Nucleostemin knockdown caused cell cycle arrest 48,49 and modified the internal pattern of the DFC, causing the loosening of snoRNP clusters. 46 USP36 depletion GAA TTC TTG TAC TTT AAC TTT CTT GGA; 1-193 aa, 581 bp, anti-sense: ATA GAA TTC ATG AAG GCT TGT GCT GCT TGT;…”

confidence: 99%

The dynamics of the alternatively spliced NOL7 gene products and role in nucleolar architecture

Kinor

Shav‐Tal

2011

Nucleus

View full text Add to dashboard Cite

Nucleolar protein Nop25 is involved in nucleolar architecture

Cited by 12 publications

References 18 publications

The Drosophila Nol12 homologue viriato is a dMyc target that regulates nucleolar architecture and is required for dMyc-stimulated cell growth

The Drosophila Nol12 homologue viriato is a dMyc target that regulates nucleolar architecture and is required for dMyc-stimulated cell growth

Heat shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin

The dynamics of the alternatively spliced NOL7 gene products and role in nucleolar architecture

Contact Info

Product

Resources

About