Back to Search
Start Over
Nucleophosmin Is a Binding Partner of Nucleostemin in Human Osteosarcoma Cells
- Source :
- Molecular Biology of the Cell. 19:2870-2875
- Publication Year :
- 2008
- Publisher :
- American Society for Cell Biology (ASCB), 2008.
-
Abstract
- Nucleostemin (NS) is expressed in the nucleoli of adult and embryonic stem cells and in many tumors and tumor-derived cell lines. In coimmunoprecipitation experiments, nucleostemin is recovered with the tumor suppressor p53, and more recently we have demonstrated that nucleostemin exerts its role in cell cycle progression via a p53-dependent pathway. Here, we report that in human osteosarcoma cells, nucleostemin interacts with nucleophosmin, a nucleolar protein believed to possess oncogenic potential. Nucleostemin (NS) and nucleophosmin (NPM) displayed an extremely high degree of colocalization in the granular component of the nucleolus during interphase, and both proteins associated with prenucleolar bodies in late mitosis before the reformation of nucleoli. Coimmunoprecipitation experiments revealed that NS and NPM co-reside in complexes, and yeast two-hybrid experiments confirmed that they are interactive proteins, revealing the NPM-interactive region to be the 46-amino acid N-terminal domain of NS. In bimolecular fluorescence complementation studies, bright nucleolar signals were observed, indicating that these two proteins directly interact in the nucleolus in vivo. These results support the notion that cell cycle regulatory proteins congress and interact in the nucleolus, adding to the emerging concept that this nuclear domain has functions beyond ribosome production.
- Subjects :
- Nucleolus
Mitosis
Bone Neoplasms
Biology
Bimolecular fluorescence complementation
GTP-Binding Proteins
Cell Line, Tumor
medicine
Humans
Granular component
Nuclear protein
Molecular Biology
Cell Nucleus
Osteosarcoma
Nucleophosmin
Cell Cycle
Nuclear Proteins
Articles
Cell Biology
Cell cycle
Molecular biology
Protein Structure, Tertiary
Cell biology
Gene Expression Regulation, Neoplastic
Cell nucleus
medicine.anatomical_structure
Microscopy, Fluorescence
Tumor Suppressor Protein p53
Carrier Proteins
Ribosomes
Protein Binding
Subjects
Details
- ISSN :
- 19394586 and 10591524
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Molecular Biology of the Cell
- Accession number :
- edsair.doi.dedup.....07369cee41aa88b3dd6a89ed27fca6e0
- Full Text :
- https://doi.org/10.1091/mbc.e08-02-0128