ArticleOncogene2001
p53 binds the nuclear matrix in normal cells: binding involves the proline-rich domain of p53 and increases following genotoxic stress.
Article in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.
- Targeting p53 pathways: mechanisms, structures, and advances in therapy.Signal transduction and targeted therapy · 2023Pooled it
- A versatile inducible plant model system for dissecting p53 function and discovering novel interaction networks.iScience · 2026Article
- p53: from understanding its structure to advances in therapeutic targeting.Signal transduction and targeted therapy · 2026Review
- The multifunctional proline-rich domain of p53 tumor suppressor.Biochimica et biophysica acta. Reviews on cancer · 2025Review
- Human Papillomavirus 31 Tyrosine 102 Regulates Interaction with E2 Binding Partners and Episomal Maintenance.Journal of virology · 2020Article
- β-Actin facilitates etoposide-induced p53 nuclear import.Journal of biosciences · 2020Article
- SH3 domains: modules of protein-protein interactions.Biophysical reviews · 2013Review
- Actin polymerization negatively regulates p53 function by impairing its nuclear import in response to DNA damage.PloS one · 2013Article
- Coordinated regulation of p53 apoptotic targets BAX and PUMA by SMAR1 through an identical MAR element.The EMBO journal · 2010Article
- Identification and characterization of the product encoded by ORF69 of Kaposi's sarcoma-associated herpesvirus.Journal of virology · 2008Article
- The novel PIAS-like protein hZimp10 is a transcriptional co-activator of the p53 tumor suppressor.Nucleic acids research · 2007Article
- Mutant p53 proteins bind DNA in a DNA structure-selective mode.Nucleic acids research · 2005Article
- Article
- The interaction of p53 with the nuclear matrix is mediated by F-actin and modulated by DNA damage.Oncogene · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tumour suppressor p53 is a multifunctional protein important for the maintenance of genomic integrity. It is able to form molecular complexes with different DNA targets and also with cellular proteins involved in DNA transcription and DNA repair. In mammalian cells the biochemical processing of DNA occurs on a nuclear sub-structure termed the nuclear matrix. Previously Deppert and co-workers have identified p53 in association with the nuclear matrix in viral- and non-viral transformed cell lines. In the present study we demonstrate, for the first time, that p53 is bound to the nuclear matrix in primary cultures of normal mammalian cells and that this binding increases following DNA damage. Analysis of cell lines expressing structural mutants of p53 revealed that association with the nuclear matrix is independent of the tertiary and quaternary structure of p53. However, the proline-rich domain towards the N-terminus of p53 (residues 67 to 98) appeared important for binding to the nuclear matrix. This was demonstrated by TET-ON regulated expression of p53-derived constructs in p53(-/-) murine embryonic fibroblasts (MEF p53(-/-)). The proline-rich domain of p53 has potential for SH3 protein-protein interaction, and has a role in p53-mediated apoptosis and possibly base excision repair of DNA damage. We discuss our observations in relation to the ability of p53 to facilitate DNA repair and also review evidence indicating that matrix-bound p53 in SV40-transformed cells may facilitate the transforming potential of SV40 large T antigen.
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