The DOI matches its Crossref record; 60 of the 62 references it cites were found in a registry or an index, and 2 are not checked yet.
Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis.
Open accessAbstract
The basic carboxy terminus of p53 plays an important role in directing the protein into the nuclear compartment. The C terminus of the p53 molecule contains a cluster of several nuclear localization signals (NLSs) that mediate the migration of the protein into the cell nucleus. NLSI, the most active domain, is highly conserved in genetically diverged species and shares perfect homology with consensus NLS sequences found in other nuclear proteins. The other two NLSs, II and III, appear to be less effective and less conserved. Although nuclear localization is dictated primarily by the NLSs inherent in the primary amino acid sequence, the actual nuclear homing can be modified by interactions with other proteins expressed in the cell. Comparison between wild-type p53 and naturally occurring mutant p53 showed that both protein categories could migrate into the nucleus of rat primary embryonic fibroblasts by essentially similar mechanisms. Nuclear localization of both proteins was totally dependent on the existence of functional NLS domains. In COS cells, however, we found that NLS-deprived wild-type p53 molecules could migrate into the nucleus by complexing with another nuclear protein, simian virus 40 large-T antigen. Wild-type and mutant p53 proteins differentially complexed with viral or cellular proteins, which may significantly affect the ultimate compartmentalization of p53 in the cell; this finding suggests that the actual subcellular compartmentalization of proteins may differ in various cell type milieux and may largely be affected by the ability of these proteins to complex with other proteins expressed in the cell. Experiments designed to test the physiological significance of p53 subcellular localization indicated that nuclear localization of mutant p53 is essential for this protein to enhance the process of malignant transformation of partially transformed cells, suggesting that p53 functions within the cell nucleus.
Checked 2026-11-15 · 2 references not checked yet
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Cited by
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Metadata
- Authors
- Shaulsky, G., Goldfinger, N., Ben-Ze'ev, A., & Rotter, V
- Affiliations
- Weizmann Institute of Science (IL)
- ORCID
- Shaulsky, G
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1990-12
- Volume
- 10
- Issue
- 12
- Pages
- 6565-6577
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC362933
- OpenAlex
- W1806610286
- Cited by
- 356
- References
- 60
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 1 · 2023: 4 · 2022: 4 · 2021: 6 · 2020: 7 · 2019: 2 · 2018: 5 · 2017: 6 · 2016: 4 · 2015: 5 · 2014: 10 · 2013: 11 · 2012: 5
- FWCI
- 11.81
- Type
- journal article
- Language
- en
- Open access
- green
- pmc.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- Funders
- Princeton University
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- p53, nuclear localization signal, nuclear accumulation, p53 C-terminal domain, SV40 large T antigen, protein-protein interaction, subcellular localization, carcinogenesis, malignant transformation, mutant p53, embryonic fibroblasts
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cell Nucleus, Cell Transformation, Neoplastic, Chromosome Deletion, Cloning, Molecular, Humans, Molecular Sequence Data, Plasmids, Sequence Homology, Nucleic Acid, Transfection, Signal Transduction, Tumor Suppressor Protein p53, Mutagenesis, Site-Directed, Mice
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- CoChat. (2026). Citation check: Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis. https://app.cochat.ai/papers/10.1128/mcb.10.12.6565
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- Shaulsky, G., Goldfinger, N., Ben-Ze'ev, A., & Rotter, V. (1990). Nuclear accumulation of p53 protein is mediated by several nuclear localization signals and plays a role in tumorigenesis. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.10.12.6565
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
