PML protein association with specific nucleolar structures differs in normal, tumor and senescent human cells
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17428679
DOI
10.1016/j.jsb.2007.02.008
PII: S1047-8477(07)00055-X
Knihovny.cz E-resources
- MeSH
- Cell Nucleolus chemistry ultrastructure MeSH
- Cell Line MeSH
- Fibroblasts cytology MeSH
- Microscopy, Fluorescence MeSH
- HeLa Cells MeSH
- Nuclear Proteins analysis metabolism MeSH
- Humans MeSH
- Mesenchymal Stem Cells cytology MeSH
- Cell Line, Tumor MeSH
- Neoplasm Proteins analysis metabolism MeSH
- Tumor Suppressor Proteins analysis metabolism MeSH
- Neoplasms pathology MeSH
- Promyelocytic Leukemia Protein MeSH
- Cellular Senescence * MeSH
- Transcription Factors analysis metabolism MeSH
- Protein Transport MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Nuclear Proteins MeSH
- Neoplasm Proteins MeSH
- Tumor Suppressor Proteins MeSH
- PML protein, human MeSH Browser
- Promyelocytic Leukemia Protein MeSH
- Transcription Factors MeSH
Promyelocytic leukemia protein (PML), a tumor suppressor, forms in most human cell types discrete multiprotein complexes termed PML nuclear bodies. Here, we have used indirect immunofluorescence and confocal microscopy to describe various forms of a novel nuclear PML compartment associated with nucleoli that is found under growth-permitting conditions in human mesenchymal stem cells (hMSC) and skin fibroblasts but not in several immortal cell lines with defects in the p53 and pRb pathways. In addition, we found that shut-off of rRNA synthesis induced by actinomycin D causes PML translocation to the surface of segregated nucleoli. This translocation is dynamic and reversible, following changes in nucleolar activity. Intriguingly, treatment causing premature senescence restores PML binding to nucleoli-derived structures and to the surface of segregated nucleoli in HeLa cells. These findings indicate that PML may be involved in nucleolar functions of normal non-transformed or senescent cells. The absence of nucleolar PML compartment in rapidly growing tumor-derived cells suggests that PML association with the nucleolus might be important for cell-cycle regulation.
References provided by Crossref.org
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