ArticleMolecular biology of the cell2011
Characterization of MRP RNA-protein interactions within the perinucleolar compartment.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Small Molecule with Big Impact: Metarrestin Targets the Perinucleolar Compartment in Cancer Metastasis.Cells · 2024Review
- The perinucleolar compartment: structure, function, and utility in anti-cancer drug development.Nucleus (Austin, Tex.) · 2024Article
- Nuclear Compartments: An Incomplete Primer to Nuclear Compartments, Bodies, and Genome Organization Relative to Nuclear Architecture.Cold Spring Harbor perspectives in biology · 2022Review
- CELF Family Proteins in Cancer: Highlights on the RNA-Binding Protein/Noncoding RNA Regulatory Axis.International journal of molecular sciences · 2021Review
- Safety assessment of metarrestin in dogs: A clinical candidate targeting a subnuclear structure unique to metastatic cancer cells.Regulatory toxicology and pharmacology : RTP · 2020Article
- Pharmacokinetic evaluation of the PNC disassembler metarrestin in wild-type and Pdx1-Cre;LSL-KrasCancer chemotherapy and pharmacology · 2018Article
- Metarrestin, a perinucleolar compartment inhibitor, effectively suppresses metastasis.Science translational medicine · 2018Article
- A small molecule inhibitor of the perinucleolar compartment, ML246, attenuates growth and spread of ovarian cancer.Gynecologic oncology research and practice · 2018Article
- Article
- Review
- New insights into functional roles of the polypyrimidine tract-binding protein.International journal of molecular sciences · 2013Review
- Environmental cues induce a long noncoding RNA-dependent remodeling of the nucleolus.Molecular biology of the cell · 2013Article
- The perinucleolar compartment associates with malignancy.Frontiers in biology · 2013Article
- The perinucleolar compartment: RNA metabolism and cancer.Cancer treatment and research · 2013Article
- Analysis of tubulin alpha-1A/1B C-terminal tail post-translational poly-glutamylation reveals novel modification sites.Journal of proteome research · 2012Article
- Putative biomarkers and targets of estrogen receptor negative human breast cancer.International journal of molecular sciences · 2011Review
- Structure and function of the perinucleolar compartment in cancer cells.Cold Spring Harbor symposia on quantitative biology · 2010Article
- CELFish ways to modulate mRNA decay.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.