scholarly journals The Perinucleolar Compartment

2010 ◽  
Vol 2 (2) ◽  
pp. a000679-a000679 ◽  
Author(s):  
C. Pollock ◽  
S. Huang
Keyword(s):  
Perinucleolar Compartment

scholarly journals The Perinucleolar Compartment and Transcription

1998 ◽  
Vol 143 (1) ◽  
pp. 35-47 ◽  
Author(s):  
Sui Huang ◽  
Thomas J. Deerinck ◽  
Mark H. Ellisman ◽  
David L. Spector
Keyword(s):  
Nucleic Acids ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Rna Polymerase Iii ◽  
Selective Inhibition ◽  
Rna Polymerases ◽  
Double Labeling ◽  
Polypyrimidine Tract Binding Protein ◽  
Cell Biol ◽  
Perinucleolar Compartment

The perinucleolar compartment (PNC) is a unique nuclear structure localized at the periphery of the nucleolus. Several small RNAs transcribed by RNA polymerase III and two hnRNP proteins have been localized in the PNC (Ghetti, A., S. Piñol-Roma, W.M. Michael, C. Morandi, and G. Dreyfuss. 1992. Nucleic Acids Res. 20:3671–3678; Matera, A.G., M.R. Frey, K. Margelot, and S.L. Wolin. 1995. J. Cell Biol. 129:1181– 1193; Timchenko, L.T., J.W. Miller, N.A. Timchenko, D.R. DeVore, K.V. Datar, L. Lin, R. Roberts, C.T. Caskey, and M.S. Swanson. 1996. Nucleic Acids Res. 24: 4407–4414; Huang, S., T. Deerinck, M.H. Ellisman, and D.L. Spector. 1997. J. Cell Biol. 137:965–974). In this report, we show that the PNC incorporates Br-UTP and FITC-conjugated CTP within 5 min of pulse labeling. Selective inhibition of RNA polymerase I does not appreciably affect the nucleotide incorporation in the PNC. Inhibition of all RNA polymerases by actinomycin D blocks the incorporation completely, suggesting that Br-UTP incorporation in the PNC is due to transcription by RNA polymerases II and/or III. Treatment of cells with an RNA polymerase II and III inhibitor induces a significant reorganization of the PNC. In addition, double labeling experiments showed that poly(A) RNA and some of the factors required for pre-mRNA processing were localized in the PNC in addition to being distributed in their previously characterized nucleoplasmic domains. Fluorescence recovery after photobleaching (FRAP) analysis revealed a rapid turnover of polypyrimidine tract binding protein within the PNC, demonstrating the dynamic nature of the structure. Together, these findings suggest that the PNC is a functional compartment involved in RNA metabolism in the cell nucleus.

scholarly journals Automated High-Content Screening for Compounds That Disassemble the Perinucleolar Compartment

2009 ◽  
Vol 14 (9) ◽  
pp. 1045-1053 ◽  
Author(s):  
John T. Norton ◽  
Steven A. Titus ◽  
Dwayne Dexter ◽  
Christopher P. Austin ◽  
Wei Zheng ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Cellular Proliferation ◽  
Rna Binding ◽  
Fluorescent Protein ◽  
Rna Binding Proteins ◽  
High Content Screening ◽  
Screening Assay ◽  
Phenotypic Marker ◽  
Perinucleolar Compartment

All solid malignancies share characteristic traits, including unlimited cellular proliferation, evasion of immune regulation, and the propensity to metastasize. The authors have previously described that a subnuclear structure, the perinucleolar compartment (PNC), is associated with the metastatic phenotype in solid tumor cancer cells. The percentage of cancer cells that contain PNCs (PNC prevalence) is indicative of the malignancy of a tumor both in vitro and in vivo, and thus PNC prevalence is a marker that reflects metastatic capability in a population of tumor cells. Although the function of the PNC remains to be determined, the PNC is highly enriched with small RNAs and RNA binding proteins. The initial chemical biology studies using a set of anticancer drugs that disassemble PNCs revealed a direct association of the structure with DNA. Therefore, PNC prevalence reduction as a phenotypic marker can be used to identify compounds that target cellular processes required for PNC maintenance and hence used to elucidate the nature of the PNC function. Here the authors report the development of an automated high-content screening assay that is capable of detecting PNC prevalence in prostate cancer cells (PC-3M) stably expressing a green fluorescent protein (GFP)—fusion protein that localizes to the PNC. The assay was optimized using known PNC-reducing drugs and non-PNC-reducing cytotoxic drugs. After optimization, the fidelity of the assay was probed with a collection of 8284 compounds and was shown to be robust and capable of detecting known and novel PNC-reducing compounds, making it the first reported high-content phenotypic screen for small changes in nuclear structure. ( Journal of Biomolecular Screening 2009:1045-1053)

scholarly journals Structure and Function of the Perinucleolar Compartment in Cancer Cells

2010 ◽  
Vol 75 (0) ◽  
pp. 599-605 ◽  
Author(s):  
A. Slusarczyk ◽  
R. Kamath ◽  
C. Wang ◽  
D. Anchel ◽  
C. Pollock ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Structure And Function ◽  
Perinucleolar Compartment ◽  
And Function

scholarly journals The Perinucleolar Compartment Is Directly Associated with DNA

2008 ◽  
Vol 284 (7) ◽  
pp. 4090-4101 ◽  
Author(s):  
John T. Norton ◽  
Chen Wang ◽  
Alison Gjidoda ◽  
R. William Henry ◽  
Sui Huang
Keyword(s):  
Perinucleolar Compartment

scholarly journals The perinucleolar compartment associates with malignancy

2013 ◽  
Vol 8 (4) ◽  
pp. 369-376 ◽  
Author(s):  
Yiping Wen ◽  
Chen Wang ◽  
Sui Huang
Keyword(s):  
Perinucleolar Compartment

scholarly journals Self-Renewal Signalling in Presenescent Tetraploid IMR90 Cells

2011 ◽  
Vol 2011 ◽  
pp. 1-14 ◽  
Author(s):  
Anda Huna ◽  
Kristine Salmina ◽  
Elina Jascenko ◽  
Gunars Duburs ◽  
Inna Inashkina ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Normal Human Fibroblast ◽  
Malignant Growth ◽  
Self Renewal ◽  
Perinucleolar Compartment ◽  
Damage Response ◽  
Molecular Context ◽  
Normal Human ◽  
Fibroblast Model

Endopolyploidy and genomic instability are shared features of both stress-induced cellular senescence and malignant growth. Here, we examined these facets in the widely used normal human fibroblast model of senescence, IMR90. At the presenescence stage, a small (2–7%) proportion of cells overcome the 4n-G1 checkpoint, simultaneously inducing self-renewal (NANOG-positivity), the DNA damage response (DDR; γ-H2AX-positive foci), and senescence (p16inka4a- and p21CIP1-positivity) signalling, some cells reach octoploid DNA content and divide. All of these markers initially appear and partially colocalise in the perinucleolar compartment. Further, with development of senescence and accumulation of p16inka4a and p21CIP1, NANOG is downregulated in most cells. The cells increasingly arrest in the 4n-G1 fraction, completely halt divisions and ultimately degenerate. A positive link between DDR, self-renewal, and senescence signalling is initiated in the cells overcoming the tetraploidy barrier, indicating that cellular and molecular context of induced tetraploidy during this period of presenescence is favourable for carcinogenesis.

scholarly journals Characterization of MRP RNA–protein interactions within the perinucleolar compartment

2011 ◽  
Vol 22 (6) ◽  
pp. 858-866 ◽  
Author(s):  
Callie Pollock ◽  
Kelly Daily ◽  
Van Trung Nguyen ◽  
Chen Wang ◽  
Marzena Anna Lewandowska ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Rna Binding ◽  
Fluorescent Protein ◽  
Gene Expression Regulation ◽  
Rna Binding Proteins ◽  
Binding Protein ◽  
Mitochondrial Rna ◽  
Human Telomerase Reverse Transcriptase ◽  
Perinucleolar Compartment

The perinucleolar compartment (PNC) forms in cancer cells and is highly enriched with a subset of polymerase III RNAs and RNA-binding proteins. Here we report that PNC components mitochondrial RNA–processing (MRP) RNA, pyrimidine tract–binding protein (PTB), and CUG-binding protein (CUGBP) interact in vivo, as demonstrated by coimmunoprecipitation and RNA pull-down experiments. Glycerol gradient analyses show that this complex is large and sediments at a different fraction from known MRP RNA–containing complexes, the MRP ribonucleoprotein ribozyme and human telomerase reverse transcriptase. Tethering PNC components to a LacO locus recruits other PNC components, further confirming the in vivo interactions. These interactions are present both in PNC-containing and -lacking cells. High-resolution localization analyses demonstrate that MRP RNA, CUGBP, and PTB colocalize at the PNC as a reticulated network, intertwining with newly synthesized RNA. Furthermore, green fluorescent protein (GFP)–PTB and GFP-CUGBP show a slower rate of fluorescence recovery after photobleaching at the PNC than in the nucleoplasm, illustrating the different molecular interaction of the complexes associated with the PNC. These findings support a working model in which the MRP RNA–protein complex becomes nucleated at the PNC in cancer cells and may play a role in gene expression regulation at the DNA locus that associates with the PNC.

Sign in / Sign up

Export Citation Format

Share Document