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Tumor formation and inactivation of RIZ1, an Rb-binding member of a nuclear protein-methyltransferase superfamily
Open accessAbstract
The retinoblastoma protein-interacting zinc finger gene RIZ (PRDM2) is a member, by sequence homology, of a nuclear protein-methyltransferase (MTase) superfamily involved in chromatin-mediated gene expression. The gene produces two protein products, RIZ1 that contains a conserved MTase domain and RIZ2 that lacks the domain. RIZ1 gene expression is frequently silenced in human cancers, and the gene is also a common target of frameshift mutation in microsatellite-unstable cancers. We now report studies of mice with a targeted mutation in the RIZ1 locus. The mutation inactivates RIZ1 but not RIZ2. These RIZ1 mutant mice were viable and fertile but showed a high incidence of diffuse large B-cell lymphomas (DLBL) and a broad spectrum of unusual tumors. RIZ1 deficiency also accelerated tumorigenesis in p53 heterozygous mutant mice. Finally, several missense mutations of RIZ1 were found in human tumor tissues and cell lines; one of these was particularly common in human DLBL tumors. These missense mutations, as well as the previously described frameshift mutation, all mapped to the MTase functional domains. All abolished the capacity of RIZ1 to enhance estrogen receptor activation of transcription. These data suggest a direct link between tumor formation and the MTase domain of RIZ1 and describe for the first time a tumor susceptibility gene among methyltransferases.
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“However, Rb can interact with other histone methyltransferases (Steele-Perkins et al., 2001)”
From Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence (2003) · cites this paper as Steele-Perkins et al., 2001
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Metadata
- Authors
- Steele-Perkins, G., Fang, W., Yang, X.-H., Van Gele, M., Carling, T., Gu, J., Buyse, I. M., Fletcher, J. A., Liu, J., Bronson, R., Chadwick, R. B., de la Chapelle, A., Zhang, X.-K., Speleman, F., & Huang, S.
- Affiliations
- Cleveland Clinic (US)
- Tufts University (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2001-09-01
- Volume
- 15
- Issue
- 17
- Pages
- 2250-2262
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC312773
- OpenAlex
- W2166083262
- Cited by
- 208
- References
- 52
- Citations by year
- 2025: 4 · 2024: 3 · 2023: 4 · 2022: 1 · 2021: 4 · 2020: 2 · 2019: 3 · 2018: 6 · 2017: 12 · 2016: 8 · 2015: 15 · 2014: 8 · 2013: 9 · 2012: 10
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- Funders
- Tobacco-Related Disease Research Program
- National Institutes of Health (5r01ca076146-03)
- National Cancer Institute (CA-76146, CA60988, R01CA060988)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- RIZ1, PRDM2, cancer susceptibility genes, diffuse large B-cell lymphoma, carcinogenesis, microsatellite instability, frameshift mutation, missense mutations
- MeSH terms
- Alleles, Amino Acid Sequence, Animals, Base Sequence, DNA Mutational Analysis, DNA-Binding Proteins, Multigene Family, Heterozygote, Humans, Immunoglobulin Heavy Chains, Karyotyping, Models, Genetic, Molecular Sequence Data, Mutation, Neoplasms, Nuclear Proteins, Protein Binding, Histone-Lysine N-Methyltransferase, Receptors, Estrogen, Time Factors, Transcription Factors, Tumor Cells, Cultured, Blotting, Southern, Blotting, Northern, Transcriptional Activation, Genes, p53, Retinoblastoma Protein, Mutagenesis, Site-Directed, Frameshift Mutation, Protein Structure, Tertiary, Microsatellite Repeats, Genetic Predisposition to Disease, Mutation, Missense, Reverse Transcriptase Polymerase Chain Reaction, Mice
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