The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation
Abstract
Changes in the substrate specificities of factors that irreversibly modify the histone components of chromatin are expected to have a profound effect on gene expression through epigenetics. Ezh2 is a histone-lysine methyltransferase with activity dependent on its association with other components of the Polycomb Repressive Complexes 2 and 3 (PRC2/3). Ezh2 levels are increasingly elevated during prostate cancer progression. Other PRC2/3 components also are elevated in cancer cells. Overexpression of Ezh2 in tissue culture promotes formation of a previously undescribed PRC complex, PRC4, that contains the NAD + -dependent histone deacetylase SirT1 and isoform 2 of the PRC component Eed. Eed2 is expressed in cancer and undifferentiated embryonic stem (ES) cells but is undetectable in normal and differentiated ES cells. The distinct PRCs exhibit differential histone substrate specificities. These findings suggest that formation of a transformation-specific PRC complex may have a major role in resetting patterns of gene expression by regulating chromatin structure.
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“HPV-16 E7 has also been shown to induce expression of H3K27 histone methyltransferase EZH2 (enzymatic component of PRC2), enhancing PRC4 complex formation [337], which has been demonstrated to cause histone H1K26 deacetylation and methylation [338]”
From The Not-So-Good, the Bad and the Ugly: HPV E5, E6 and E7 Oncoproteins in the Orchestration of Carcinogenesis (2021) · cites this paper as [338]
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Cites
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
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The polycomb group protein EZH2 is involved in progression of prostate cancer
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EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer.
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Cited by
Ohm, J. E., McGarvey, K. M., Yu, X., Cheng, L., Schuebel, K. E., Cope, L., Mohammad, H. P., Chen, W., Daniel, V. C., Yu, W., et al. (2007) · Nature Genetics · doi:10.1038/ng1972 · Cited by 1,130
Tan, J., Yang, X., Zhuang, L., Jiang, X., Chen, W., Lee, P. L., Karuturi, R. K. M., Tan, P. B. O., Liu, E. T., & Yu, Q. (2007) · Genes & Development · doi:10.1101/gad.1524107 · Cited by 895
Chromatin higher-order structures and gene regulation
Li, G., & Reinberg, D. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.01.022 · Cited by 454
Self-citationO'Hagan, H. M., Mohammad, H. P., & Baylin, S. B. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000155 · Cited by 386
Inhibition of SIRT1 Reactivates Silenced Cancer Genes without Loss of Promoter DNA Hypermethylation
Pruitt, K., Zinn, R. L., Ohm, J. E., McGarvey, K. M., Kang, S.-H. L., Watkins, D. N., Herman, J. G., & Baylin, S. B. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020040 · Cited by 387
“First, there are data suggesting high expression of this protein in a number of cancer cell lines [49,50], and we have observed this as well (unpublished data and [51]).”
BackgroundPolycomb Group Protein Ezh2 Controls Actin Polymerization and Cell Signaling
Su, I.-H., Dobenecker, M.-W., Dickinson, E., Oser, M., Basavaraj, A., Marqueron, R., Viale, A., Reinberg, D., Wülfing, C., & Tarakhovsky, A. (2005) · Cell · doi:10.1016/j.cell.2005.02.029 · Cited by 365
Self-citationCross‐Talk between Aging and Cancer: The Epigenetic Language
FRAGA, M. F., AGRELO, R., & ESTELLER, M. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1395.005 · Cited by 251
Polycomb Repressive Complex 2 and Trithorax modulate Drosophila longevity and stress resistance
Siebold, A. P., Banerjee, R., Tie, F., Kiss, D. L., Moskowitz, J., & Harte, P. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907739107 · Cited by 216
Basukala, O., & Banks, L. (2021) · Viruses · doi:10.3390/v13101892 · Cited by 137
Sirtuin‐dependent epigenetic regulation in the maintenance of genome integrity
Bosch‐Presegué, L., & Vaquero, A. (2015) · The FEBS Journal · doi:10.1111/febs.13053 · Cited by 132
Self-citationThe Osteoblast to Osteocyte Transition: Epigenetic Changes and Response to the Vitamin D3Hormone
St. John, H. C., Bishop, K. A., Meyer, M. B., Benkusky, N. A., Leng, N., Kendziorski, C., Bonewald, L. F., & Pike, J. W. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1091 · Cited by 127
Polycomb proteins in hematologic malignancies
Martin-Perez, D., Piris, M. A., & Sanchez-Beato, M. (2010) · Blood · doi:10.1182/blood-2010-05-267096 · Cited by 65
Metadata
- Authors
- Kuzmichev, A., Margueron, R., Vaquero, A., Preissner, T. S., Scher, M., Kirmizis, A., Ouyang, X., Brockdorff, N., Abate-Shen, C., Farnham, P., & Reinberg, D.
- Affiliations
- Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, and Center for Advanced Biotechnology and Medicine, Department of Medicine and Cancer Institute of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854; X Inactivation Group Medical Research Council Clinical Sciences Centre, Imperial College School of Medicine Hammersmith Hospital, London W12 0NN, United Kingdom; and McArdle Laboratory for Cancer Research, University of Wisconsin...
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2005-01-31
- Volume
- 102
- Issue
- 6
- Pages
- 1859-1864
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 336
- References
- 4
- Language
- en
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