JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
Abstract
JHDM1B is an evolutionarily conserved and ubiquitously expressed member of the JHDM (JmjC-domain-containing histone demethylase) family. Because it contains an F-box motif, this protein is also known as FBXL10 (ref. 4). With the use of a genome-wide RNAi screen, the JHDM1B worm orthologue (T26A5.5) was identified as a gene that regulates growth. In the mouse, four independent screens have identified JHDM1B as a putative tumour suppressor by retroviral insertion analysis. Here we identify human JHDM1B as a nucleolar protein and show that JHDM1B preferentially binds the transcribed region of ribosomal DNA to repress the transcription of ribosomal RNA genes. We also show that repression of ribosomal RNA genes by JHDM1B is dependent on its JmjC domain, which is necessary for the specific demethylation of trimethylated lysine 4 on histone H3 in the nucleolus. In agreement with the notion that ribosomal RNA synthesis and cell growth are coupled processes, we show a JmjC-domain-dependent negative effect of JHDM1B on cell size and cell proliferation. Because aberrant ribosome biogenesis and the disruption of epigenetic control mechanisms contribute to cellular transformation, these results, together with the low levels of JHDM1B expression found in aggressive brain tumours, suggest a role for JHDM1B in cancer development.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Inactivating mutations and/or reduced expression of JmjC histone demethylases including JARID1C, UTX and JHDM1B/FBXL10 occur in renal cell carcinomas, multiple myeloma, glioblastoma multiforme and several other cancers.
“Interestingly, inactivating mutations and/or reduced expression of JmjC histone demethylases including JARID1C (Dalgliesh et al, 2010), UTX (van Haaften et al, 2009) and JHDM1B/FBXL10 (Frescas et al, 2007), occur in RCCs, multiple myeloma, glioblastoma multiforme and several other cancers.”
From The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases (2011) · cites this paper as Frescas et al, 2007
Cites
Histone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,171 · see citing works
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290 · see citing works
Does the ribosome translate cancer?
Ruggero, D., & Pandolfi, P. P. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1015 · Cited by 924 · see citing works
Gene Expression Profiling of Gliomas Strongly Predicts Survival
Freije, W. A., Castro-Vargas, F. E., Fang, Z., Horvath, S., Cloughesy, T. F., Liau, L. M., Mischel, P. S., & Nelson, S. F. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0452 · Cited by 745 · see citing works
Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J.-I., Saijo, M., Drapkin, R., Kisselev, A. F., Tanaka, K., & Nakatani, Y. (2003) · Cell · doi:10.1016/s0092-8674(03)00316-7 · Cited by 739 · see citing works
The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
Cloos, P. A., Christensen, J., Agger, K., Maiolica, A., Rappsilber, J., Antal, T., Hansen, K. H., & Helin, K. (2006) · Nature · doi:10.1038/nature04837 · Cited by 738 · see citing works
S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth
Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731 · see citing works
Self-citationSystematic analysis and nomenclature of mammalian F-box proteinsPreprint
Jin, J., Cardozo, T. J., Lovering, R. C., Elledge, S. J., Pagano, M., & Harper, J. W. (2004) · Genes & Development · doi:10.1101/gad.1255304 · Cited by 716 · see citing works
Self-citationDynamic Regulation of Histone Lysine Methylation by Demethylases
Shi, Y., & Whetstine, J. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.010 · Cited by 710 · see citing works
c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I
Grandori, C., Gomez-Roman, N., Felton-Edkins, Z. A., Ngouenet, C., Galloway, D. A., Eisenman, R. N., & White, R. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1224 · Cited by 659 · see citing works
Busino, L., Bassermann, F. C., Maiolica, A., Lee, C., Nolan, P. M., Godinho, S. I. H., Draetta, G. F., & Pagano, M. (2007) · Science · doi:10.1126/science.1141194 · Cited by 509 · see citing works
Self-citationControl of the SCFSkp2–Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase
Bashir, T., Dorrello, N. V., Amador, V., Guardavaccaro, D., & Pagano, M. (2004) · Nature · doi:10.1038/nature02330 · Cited by 504 · see citing works
Self-citationc-Myc associates with ribosomal DNA and activates RNA polymerase I transcription
Arabi, A., Wu, S., Ridderstråle, K., Bierhoff, H., Shiue, C.-N., Fátyol, K., Fahlén, S., Hydbring, P., Söderberg, O., Grummt, I., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1225 · Cited by 471 · see citing works
New genes involved in cancer identified by retroviral tagging
Suzuki, T., Shen, H., Akagi, K., Morse, H. C., Malley, J. D., Naiman, D. Q., Jenkins, N. A., & Copeland, N. G. (2002) · Nature Genetics · doi:10.1038/ng949 · Cited by 420 · see citing works
Bredel, M., Bredel, C., Juric, D., Harsh, G. R., Vogel, H. S., Recht, L. D., & Sikic, B. I. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1204 · Cited by 311 · see citing works
Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259 · see citing works
Earley, K. W., Lawrence, R. J., Pontes, O., Reuther, R. A., Enciso, A. J., Silva, M., Neves, N., Gross, M. L., Viegas, W. S., & Pikaard, C. S. (2006) · Genes & Development · doi:10.1101/gad.1417706 · Cited by 240 · see citing works
Leukaemia disease genes: large-scale cloning and pathway predictions
Li, J., Shen, H., Himmel, K. L., Dupuy, A. J., Largaespada, D. A., Nakamura, T., Shaughnessy, J. D., Jenkins, N. A., & Copeland, N. G. (1999) · Nature Genetics · doi:10.1038/15531 · Cited by 237 · see citing works
Identification of genes that protect theC. elegansgenome against mutations by genome-wide RNAiPreprint
Pothof, J., van Haaften, G. W., Thijssen, K. L., Kamath, R. S., Fraser, A. G., Ahringer, J., Plasterk, R. H. A., & Tijsterman, M. (2003) · Genes & Development · doi:10.1101/gad.1060703 · Cited by 213 · see citing works
APC/CCdc20 Controls the Ubiquitin-Mediated Degradation of p21 in Prometaphase
Amador, V., Ge, S., Santamarı́a, P. G., Guardavaccaro, D., & Pagano, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.013 · Cited by 209 · see citing works
Self-citationVoo, K. S., Carlone, D. L., Jacobsen, B. M., Flodin, A., & Skalnik, D. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2108-2121.2000 · Cited by 194 · see citing works
Stress-Dependent Nucleolin Mobilization Mediated by p53-Nucleolin Complex Formation
Daniely, Y., Dimitrova, D. D., & Borowiec, J. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.6014-6022.2002 · Cited by 170 · see citing works
Leung, A. K. L., Gerlich, D. W., Miller, G., Lyon, C. E., Lam, Y. W., Llères, D., Daigle, N., Zomerdijk, J. C. B. M., Ellenberg, J., & Lamond, A. I. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405013 · Cited by 169 · see citing works
Preuss, S. B., & Pikaard, C. S. (2007) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2007.02.005 · Cited by 150 · see citing works
Tumor suppressor gene identification using retroviral insertional mutagenesis in Blm‐deficient mice
Suzuki, T., Minehata, K., Akagi, K., Jenkins, N. A., & Copeland, N. G. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601215 · Cited by 148 · see citing works
Initiation of Nucleolar Assembly Is Independent of RNA Polymerase I Transcription
Dousset, T., Wang, C., Verheggen, C., Chen, D., Hernandez‐Verdun, D., & Huang, S. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.8.2705 · Cited by 136 · see citing works
Hwang, H. C., Martins, C. P., Bronkhorst, Y., Randel, E., Berns, A. J. M., Fero, M. L., & Clurman, B. E. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162356099 · Cited by 106 · see citing works
Frescas, D., Mavrakis, M., Lorenz, H., DeLotto, R., & Lippincott‐Schwartz, J. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601156 · Cited by 76 · see citing works
Self-citationThe F-box protein Fbl10 is a novel transcriptional repressor of c-Jun
Koyama‐Nasu, R., David, G., & Tanese, N. (2007) · Nature Cell Biology · doi:10.1038/ncb1628 · Cited by 61 · see citing works
Self-citationMosaic methylation of the repeat unit of the human ribosomal RNA genes
Brock, G., & Bird, A. P. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.3.451 · Cited by 53 · see citing works
Flagged first, then by citations
1 of the 31 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241 · see citing works
Covalent histone modifications — miswritten, misinterpreted and mis-erased in human cancers
Chi, P., Allis, C. D., & Wang, G. G. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2876 · Cited by 1,099 · see citing works
The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases
Chowdhury, R., Yeoh, K. K., Tian, Y., Hillringhaus, L., Bagg, E. A., Rose, N. R., Leung, I. K. H., Li, X. S., Woon, E. C. Y., Yang, M., et al. (2011) · The EMBO Reports · doi:10.1038/embor.2011.43 · Cited by 1,035 · see citing works
Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer
Frescas, D., & Pagano, M. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2396 · Cited by 886 · see citing works
Self-citationMolecular mechanisms and potential functions of histone demethylases
Kooistra, S. M., & Helin, K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3327 · Cited by 882 · see citing works
Biogenesis and function of nuclear bodies
Mao, Y. S., Zhang, B., & Spector, D. L. (2011) · Trends in Genetics · doi:10.1016/j.tig.2011.05.006 · Cited by 707 · see citing works
Histone ubiquitination: triggering gene activity.
Weake, V. M., & Workman, J. (2008) · Molecules and Cells · doi:10.1016/j.molcel.2008.02.014 · Cited by 742 · see citing works
Erasing the methyl mark: histone demethylases at the center of cellular differentiation and diseasePreprint
Cloos, P. A., Christensen, J., Agger, K., & Helin, K. (2008) · Genes & Development · doi:10.1101/gad.1652908 · Cited by 664 · see citing works
What a difference a hydroxyl makes: mutant IDH, (<i>R</i>)-2-hydroxyglutarate, and cancer
Losman, J.-A., & Kaelin, W. G. (2013) · Genes & Development · doi:10.1101/gad.217406.113 · Cited by 570 · see citing works
The Epigenetics of rRNA Genes: From Molecular to Chromosome Biology
McStay, B., & Grummt, I. (2008) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.24.110707.175259 · Cited by 527 · see citing works
Roles of F-box proteins in cancer
Wang, Z. P., Liu, P., Inuzuka, H., & Wei, W. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3700 · Cited by 516 · see citing works
KDM2B links the Polycomb Repressive Complex 1 (PRC1) to recognition of CpG islands
Farcas, A. M., Blackledge, N. P., Sudbery, I. M., Long, H. K., McGouran, J. F., Rose, N. R., Lee, S., Sims, D., Cerase, A., Sheahan, T. W., et al. (2012) · eLife · doi:10.7554/elife.00205 · Cited by 472 · see citing works
Vitamin C: Update on physiology and pharmacology
Mandl, J., Szarka, A., & Bánhegyi, G. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00282.x · Cited by 451 · see citing works
The Cdc14B-Cdh1-Plk1 Axis Controls the G2 DNA-Damage-Response Checkpoint
Bassermann, F., Frescas, D., Guardavaccaro, D., Busino, L., Peschiaroli, A., & Pagano, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.043 · Cited by 397 · see citing works
Self-citationHistone demethylases in development and disease
Pedersen, M. T., & Helin, K. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.08.011 · Cited by 389 · see citing works
Yu, X., Li, L., Li, L., Guo, M., Chory, J., & Yin, Y. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802254105 · Cited by 341 · see citing works
Histone lysine methylation and demethylation pathways in cancer
Varier, R. A., & Timmers, H. T. M. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.10.002 · Cited by 338 · see citing works
Inhibitors of Protein Methyltransferases and Demethylases
Kanıskan, H. Ü., Martini, M. L., & Jin, J. J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00801 · Cited by 320 · see citing works
Targeting epigenetic regulators to overcome drug resistance in cancers
Wang, N., Ma, T., & Yu, B. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01341-7 · Cited by 319 · see citing works
Fetahu, I. S., Höbaus, J., & Kállay, E. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00164 · Cited by 313 · see citing works
CpG Islands Recruit a Histone H3 Lysine 36 Demethylase
Blackledge, N. P., Zhou, J., Tolstorukov, M. Y., Farcas, A. M., Park, P. J., & Klose, R. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.009 · Cited by 310 · see citing works
The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15Ink4b
He, J., Kallin, E. M., Tsukada, Y.-I., & Zhang, Y. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1499 · Cited by 295 · see citing works
dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencingPreprint
Lagarou, A., Mohd-Sarip, A., Moshkin, Y. M., Chalkley, G. E., Bezstarosti, K., Demmers, J., & Verrijzer, C. P. (2008) · Genes & Development · doi:10.1101/gad.484208 · Cited by 260 · see citing works
Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing
Webb, J. D., Coleman, M. L., & Pugh, C. W. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0147-7 · Cited by 255 · see citing works
BCOR regulates mesenchymal stem cell function by epigenetic mechanisms
Fan, Z., Yamaza, T., Lee, J. S., Yu, J., Wang, S., Fan, G., Shi, S., & Wang, C.-Y. (2009) · Nature Cell Biology · doi:10.1038/ncb1913 · Cited by 246 · see citing works
Mechanisms involved in the regulation of histone lysine demethylases
Lan, F., Nottke, A. C., & Shi, Y. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.004 · Cited by 241 · see citing works
Smith, E. R., & Shilatifard, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.031 · Cited by 234 · see citing works
Lysine methylation: beyond histones
Zhang, X., Wen, H., & Shi, X. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr100 · Cited by 233 · see citing works
The emerging functions of histone demethylases
Agger, K., Christensen, J. F., Cloos, P. A., & Helin, K. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2007.12.003 · Cited by 231 · see citing works
2-Oxoglutarate-dependent dioxygenases in cancer
Losman, J.-A., Koivunen, P., & Kaelin, W. G. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-00303-3 · Cited by 225 · see citing works
Dynamic protein methylation in chromatin biology
Ng, S. S., Yue, W. W., Oppermann, U. C. T., & Klose, R. J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8303-z · Cited by 226 · see citing works
PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
Feng, W., Yonezawa, M., Ye, J., Jenuwein, T., & Grummt, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1778 · Cited by 219 · see citing works
Tumor hypoxia: From basic knowledge to therapeutic implications
Liao, C., Liu, X., Zhang, C., & Zhang, Q. (2023) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.12.011 · Cited by 223 · see citing works
Epigenetic regulation of the<i>INK4b-ARF-INK4a</i>locus: In sickness and in health
Popov, N., & Gil, J. (2010) · Epigenetics · doi:10.4161/epi.5.8.12996 · Cited by 202 · see citing works
Basic mechanisms in RNA polymerase i transcription of the ribosomal RNA genes
Goodfellow, S. J., & Zomerdijk, J. C. B. M. (2013) · Subcellular Biochemistry · doi:10.1007/978-94-007-4525-4_10 · Cited by 197 · see citing works
Targeting Histone Demethylases: A New Avenue for the Fight against Cancer
Rotili, D., & Mai, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417976 · Cited by 192 · see citing works
RNA polymerases I and III, non-coding RNAs and cancer
White, R. J. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.10.003 · Cited by 190 · see citing works
Molenaar, R. J., Radivoyevitch, T., Maciejewski, J. P., Noorden, C. J. F. V., & Bleeker, F. E. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.05.004 · Cited by 181 · see citing works
Cohen, M. M., Leboucher, G. P., Livnat‐Levanon, N., Glickman, M. H., & Weissman, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0227 · Cited by 170 · see citing works
Roles of H3K4 methylation in biology and disease
Wang, H., & Helin, K. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.06.001 · Cited by 167 · see citing works
Hashemi, M., Arani, H. Z., Orouei, S., Fallah, S., Ghorbani, A., Khaledabadi, M., Kakavand, A., Tavakolpournegari, A., Saebfar, H., Heidari, H., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113774 · Cited by 167 · see citing works
The Roles of Jumonji-Type Oxygenases in Human Disease
Johansson, C., Tumber, A., Che, K., Cain, P., Nowak, R. P., Gileadi, C., & Oppermann, U. C. T. (2014) · Epigenomics · doi:10.2217/epi.13.79 · Cited by 163 · see citing works
Nagamachi, A., Matsui, H., Asou, H., Ozaki, Y., Aki, D., Kanai, A., Takubo, K., Suda, T., Nakamura, T., Wolff, L., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.08.011 · Cited by 155 · see citing works
FBXL10 protects Polycomb-bound genes from hypermethylation
Boulard, M., Edwards, J. R., & Bestor, T. H. (2015) · Nature Genetics · doi:10.1038/ng.3272 · Cited by 153 · see citing works
Interplay Between Different Epigenetic Modifications and Mechanisms
Murr, R. (2010) · Advances in genetics · doi:10.1016/b978-0-12-380866-0.60005-8 · Cited by 149 · see citing works
Lysine Demethylases Inhibitors
Suzuki, T., & Miyata, N. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201048w · Cited by 146 · see citing works
Frescas, D., Roux, C. M., Aygun-Sunar, S., Gleiberman, A. S., Krasnov, P., Kurnasov, O. V., Strom, E., Virtuoso, L. P., Wrobel, M., Osterman, A. L., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614661114 · Cited by 140 · see citing works
Self-citationSalminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 142 · see citing works
Dysregulation of RNA polymerase I transcription during disease
Hannan, K. M., Sanij, E., Rothblum, L. I., Hannan, R. D., & Pearson, R. B. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.10.014 · Cited by 137 · see citing works
Frescas, D., Guardavaccaro, D., Kuchay, S., Kato, H., Poleshko, A. S., Basrur, V., Elenitoba‐Johnson, K. S. J., Katz, R. A., & Pagano, M. (2008) · Cell Cycle · doi:10.4161/cc.7.22.7062 · Cited by 136 · see citing works
Self-citationEpigenetic control of RNA polymerase I transcription in mammalian cells
Grummt, I., & Längst, G. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.10.004 · Cited by 132 · see citing works
Teven, C. M., Liu, X., Hu, N., Tang, N., Kim, S. H., Huang, E., Yang, K., Li, M., Gao, J., Liu, H. S., et al. (2011) · Stem Cells International · doi:10.4061/2011/201371 · Cited by 129 · see citing works
Histone Demethylases and Their Roles in Cancer Epigenetics
D’Oto, A., Tian, Q., Davidoff, A. M., & Yang, J. (2016) · Journal of medical oncology and therapeutics · doi:10.35841/medical-oncology.1.2.34-40 · Cited by 127 · see citing works
Ndy1/KDM2B immortalizes mouse embryonic fibroblasts by repressing the Ink4a / Arf locus
Tzatsos, A., Pfau, R., Kampranis, S. C., & Tsichlis, P. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813139106 · Cited by 127 · see citing works
Fbxl10/Kdm2b deficiency accelerates neural progenitor cell death and leads to exencephaly
Fukuda, T., Tokunaga, A., Sakamoto, R., & Yoshida, N. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.01.001 · Cited by 124 · see citing works
Tan, M.-K. M., Lim, H.-J., Bennett, E. J., Shi, Y., & Harper, J. W. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.018 · Cited by 118 · see citing works
Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4
Huang, C., Xiang, Y., Wang, Y., Li, X., Xu, L., Zhu, Z., Zhang, T., Zhu, Q., Zhang, K., Jing, N., et al. (2010) · Cell Research · doi:10.1038/cr.2010.5 · Cited by 121 · see citing works
Pfau, R., Tzatsos, A., Kampranis, S. C., Serebrennikova, O. B., Bear, S. E., & Tsichlis, P. N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711865105 · Cited by 119 · see citing works
JmjC enzyme KDM2A is a regulator of rRNA transcription in response to starvation
Tanaka, Y., Okamoto, K., Teye, K., Umata, T., Yamagiwa, N., Suto, Y., Zhang, Y., & Tsuneoka, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.56 · Cited by 113 · see citing works
Charng, W., Karaca, E., Coban‐Akdemir, Z., Gambin, T., Atik, M. M., Gu, S., Posey, J. E., Jhangiani, S. N., Muzny, D. M., Doddapaneni, H., et al. (2016) · BMC Medical Genomics · doi:10.1186/s12920-016-0208-3 · Cited by 110 · see citing works
Global gene expression of the inner cell mass and trophectoderm of the bovine blastocyst
Ozawa, M., Sakatani, M., Yao, J., Shanker, S., Yu, F., Yamashita, R., Wakabayashi, S., Nakai, K., Dobbs, K. B., Sudano, M. J., et al. (2012) · BMC Developmental Biology · doi:10.1186/1471-213x-12-33 · Cited by 108 · see citing works
CHD7 functions in the nucleolus as a positive regulator of ribosomal RNA biogenesis
Zentner, G. E., Hurd, E. A., Schnetz, M. P., Handoko, L., Wang, C., Wang, Z., Wei, C., Tesar, P. J., Hatzoglou, M., Martin, D. M., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq265 · Cited by 105 · see citing works
Different Binding Properties and Function of CXXC Zinc Finger Domains in Dnmt1 and Tet1
Frauer, C., Rottach, A., Meilinger, D., Bultmann, S., Fellinger, K., Hasenöder, S., Wang, M., Qin, W., Söding, J., Spada, F., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016627 · Cited by 103 · see citing works
Beyond ubiquitination: the atypical functions of Fbxo7 and other F-box proteins
Nelson, D. E., Randle, S. J., & Laman, H. (2013) · Open Biology · doi:10.1098/rsob.130131 · Cited by 101 · see citing works
Vitamin C – A new player in regulation of the cancer epigenome
Gillberg, L., Ørskov, A. D., Liu, M., Harsløf, L. B. S., Jones, P. A., & Grønbæk, K. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.11.001 · Cited by 100 · see citing works
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1978-z · Cited by 99 · see citing works
Chromatin and oxygen sensing in the context of JmjC histone demethylases
Shmakova, A., Batie, M., Druker, J., & Rocha, S. (2014) · Biochemical Journal · doi:10.1042/bj20140754 · Cited by 99 · see citing works
Inactive yet indispensable: the tale of Jarid2
Landeira, D., & Fisher, A. G. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.10.004 · Cited by 97 · see citing works
Kang, J., Kim, J., Kim, K., Park, J. W., Cho, H., Hahm, J. Y., Chae, Y., Kim, D., Kook, H. Y., Rhee, S., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201800242r · Cited by 97 · see citing works
Histone lysine demethylases and their functions in cancer
Sterling, J., Menezes, S. V., Abbassi, R. H., & Munoz, L. (2020) · International Journal of Cancer · doi:10.1002/ijc.33375 · Cited by 96 · see citing works
Salminen, A., Kaarniranta, K., Hiltunen, M. O., & Kauppinen, A. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.03.030 · Cited by 96 · see citing works
Lu, Y., Beezhold, K., Chang, Q., Zhang, Y., Rojanasakul, Y., Zhao, H., Castranova, V., Shi, X., & Chen, F. (2009) · Cell Cycle · doi:10.4161/cc.8.13.8927 · Cited by 94 · see citing works
Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes
Wang, W., Chen, Z., Mao, Z., Zhang, H., Ding, X., Chen, S., Zhang, X., Xu, R.-M., & Zhu, B. (2011) · EMBO Reports · doi:10.1038/embor.2011.184 · Cited by 94 · see citing works
Montanaro, L., Treré, D., & Derenzini, M. (2011) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2011.10.006 · Cited by 93 · see citing works
Wisely chosen paths – regulation of rRNA synthesis
Grummt, I. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07892.x · Cited by 93 · see citing works
The epigenetic pathways to ribosomal DNA silencing
Srivastava, R., Srivastava, R., & Ahn, S. H. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00005-16 · Cited by 90 · see citing works
Cheng, Z., Cheung, P., Kuo, A. J., Yukl, E. T., Wilmot, C. M., Gozani, O., & Patel, D. J. (2014) · Genes & Development · doi:10.1101/gad.246561.114 · Cited by 90 · see citing works
Epigenetic regulation in cancer therapy: From mechanisms to clinical advances
Tao, L., Zhou, Y., Luo, Y., Qiu, J., Xiao, Y., Zou, J., Zhang, Y., Liu, X., Yang, X., Gou, K., et al. (2024) · MedComm – Oncology · doi:10.1002/mog2.59 · Cited by 93 · see citing works
Hypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related Diseases
Salminen, A., Kai, K., & Kauppinen, A. (2016) · Aging and Disease · doi:10.14336/ad.2015.0929 · Cited by 90 · see citing works
Recent advances in SCF ubiquitin ligase complex: Clinical implications
Zheng, N., Zhou, Q., Wang, Z. P., & Wei, W. (2016) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2016.05.001 · Cited by 88 · see citing works
Emerging roles of F-box proteins in cancer drug resistance
Yan, L., Lin, M., Pan, S., Assaraf, Y. G., Wang, Z. P., & Zhu, X. (2019) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100673 · Cited by 85 · see citing works
Tian, X., Zhang, S., Liu, H., Zhang, Y., Blair, C., Mercola, D., Sassone‐Corsi, P., & Zi, X. (2013) · Current Cancer Drug Targets · doi:10.2174/1568009611313050007 · Cited by 88 · see citing works
Fichelson, P., Moch, C., Ivanovitch, K., Martin, C. A., Sidor, C., Lepesant, J., Bellaı̈che, Y., & Huynh, J. (2009) · Nature Cell Biology · doi:10.1038/ncb1874 · Cited by 87 · see citing works
Emerging Roles of JmjC Domain-Containing Proteins
Accari, S. L., & Fisher, P. R. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.003 · Cited by 87 · see citing works
Polycomb complexes PRC1 and their function in hematopoiesis
Vidal, M., & Starowicz, K. (2017) · Experimental Hematology · doi:10.1016/j.exphem.2016.12.006 · Cited by 83 · see citing works
Schöfer, C., & Weipoltshammer, K. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1696-3 · Cited by 83 · see citing works
Transcriptional Repression: Conserved and Evolved Features
Payankaulam, S., Li, L. M., & Arnosti, D. N. (2010) · Current Biology · doi:10.1016/j.cub.2010.06.037 · Cited by 79 · see citing works
Kawakami, E., Tokunaga, A., Ozawa, M., Sakamoto, R., & Yoshida, N. (2014) · Mechanisms of Development · doi:10.1016/j.mod.2014.10.001 · Cited by 78 · see citing works
Jumonji histone demethylases as emerging therapeutic targets
Park, S. Y., Park, J., & Chun, Y. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.01.026 · Cited by 74 · see citing works
Janzer, A., Stamm, K., Becker, A., Zimmer, A., Buettner, R., & Kirfel, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.341040 · Cited by 73 · see citing works
The critical role of histone lysine demethylase KDM2B in cancer.
Yan, M., Yang, X., Wang, H., & Shao, Q. (2018) · Europe PMC (PubMed Central) · Cited by 68 · see citing works
Structure and Epigenetics of Nucleoli in Comparison With Non-nucleolar Compartments
Bártová, E., Horáková, A. H., Uhlířová, R., Raška, I., Galiová, G., Orlova, D. Y., & Kozubek, S. (2009) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2009.955435 · Cited by 68 · see citing works
Subcellular compartmentation of ascorbate and its variation in disease states
Bánhegyi, G., Benedetti, A., Margittai, É., Marcolongo, P., Fulceri, R., Németh, C. E., & Szarka, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.016 · Cited by 68 · see citing works
Wang, S., Cheng, Y., Du, W., Lu, L., Zhou, L., Wang, H., Kang, W., Li, X., Tao, Q., Sung, J. J. �., et al. (2012) · Gut · doi:10.1136/gutjnl-2011-301776 · Cited by 68 · see citing works
Epigenetics: An emerging player in gastric cancer
Kang, C. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i21.6433 · Cited by 67 · see citing works
Gilder, A. S., Do, P. M., Carrero, Z. I., Cosman, A. M., Broome, H. J., Velma, V., Martinez, L. A., & Hebert, M. D. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-08-0731 · Cited by 65 · see citing works
Ubiquitination-mediated degradation of cell cycle-related proteins by F-box proteins
Zheng, N., Wang, Z. P., & Wei, W. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.02.005 · Cited by 62 · see citing works
Polytarchou, C., Pfau, R., Hatziapostolou, M., & Tsichlis, P. N. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00688-08 · Cited by 63 · see citing works
Labonne, J. D. J., Lee, K.-H., Iwase, S., Kong, I.-K., Diamond, M. P., Layman, L. C., Kim, C.-H., & Kim, H.-G. (2016) · Human Genetics · doi:10.1007/s00439-016-1668-4 · Cited by 61 · see citing works
Deregulation of F-box proteins and its consequence on cancer development, progression and metastasis
Heo, J., Eki, R., & Abbas, T. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.09.015 · Cited by 59 · see citing works
- Authors
- Frescas, D., Guardavaccaro, D., Bassermann, F., Koyama-Nasu, R., & Pagano, M.
- Affiliations
- New York University (US)
- Corresponding author
- Pagano, Michele
- Venue
- Nature
- Published
- 2007-11
- Volume
- 450
- Issue
- 7167
- Pages
- 309-313
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1975472671
- Cited by
- 284
- References
- 31
- Citations by year
- 2026: 5 · 2025: 12 · 2024: 14 · 2023: 11 · 2022: 9 · 2021: 15 · 2020: 14 · 2019: 9 · 2018: 14 · 2017: 11 · 2016: 13 · 2015: 12 · 2014: 24 · 2013: 19 · 2012: 17
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- B, histone H3 lysine 4 trimethylation, ribosomal RNA gene transcription, nucleolar proteins, tumour suppressor, ribosome biogenesis, cell proliferation, cell size, epigenetic regulation, histone demethylation, carcinogenesis
- MeSH terms
- Cell Nucleolus, DNA, Ribosomal, HeLa Cells, Histones, Humans, Methylation, Nuclear Proteins, Oxidoreductases, N-Demethylating, Repressor Proteins, Transcription, Genetic, Down-Regulation, Protein Structure, Tertiary, Genes, rRNA, RNA Interference, F-Box Proteins, Cell Proliferation, Jumonji Domain-Containing Histone Demethylases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review