Artículo

Rocha-Viegas, L.; Villa, R.; Gutierrez, A.; Iriondo, O.; Shiekhattar, R.; Croce, L.D. "Role of UTX in retinoic acid receptor-mediated gene regulation in leukemia" (2014) Molecular and Cellular Biology. 34(19):3765-3775
Estamos trabajando para incorporar este artículo al repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Human UTX, a member of the Jumonji C family of proteins, associates with mixed-lineage leukemia 3/4 complexes. Stimulation with retinoic acid leads to the recruitment of UTX-containing complexes to HOX genes, which results in demethylation of histone H3 lysine 27 and concomitant methylation of histone H3 lysine 4. Here, we show that UTX interacts with the retinoic acid receptor α (RARα) and that this interaction is essential for proper differentiation of leukemic U937 cells in response to retinoic acid. UTX occupies the promoters of several RAR target genes and regulates their transcriptional output by modulating ASH2L complex recruitment. Overexpression of UTX in promyelocytic NB4 cells results in enhanced cellular differentiation upon retinoic acid treatment. Our results show that UTX is important for RAR-mediated transcription and provide insight into the critical role of cross talk between histone H3 lysine 4 methylation and histone H3 lysine 27 demethylation during cellular differentiation. © 2014, American Society for Microbiology.

Registro:

Documento: Artículo
Título:Role of UTX in retinoic acid receptor-mediated gene regulation in leukemia
Autor:Rocha-Viegas, L.; Villa, R.; Gutierrez, A.; Iriondo, O.; Shiekhattar, R.; Croce, L.D.
Filiación:Center for Genomic Regulation, Barcelona, Spain
Universitat Pompeu Fabra, Barcelona, Spain
Sylvester Comprehensive Cancer Center, University of Miami Miller School of Medicine, Miami, FL, United States
Institucio´ Catalana de Recerca i Estudis Avanc¸ats, Barcelona, Spain
Departamento de Qui´mica Biolo´gica, FCEN, IFIBYNE-CONICET, Universidad de Buenos Aires, Buenos Aires, Argentina
Adolf Butenamdt Institut, Molecular Biology, LMU, Munich, Germany
Department of Stem Cell Biology and Regenerative Medicine, University of Southern California, Los Angeles, CA, United States
Palabras clave:histone H3; lysine; protein; retinoic acid; retinoic acid receptor alpha; unclassified drug; utx protein; antineoplastic agent; ASH2L protein, human; DNA binding protein; histone; histone demethylase; nuclear protein; retinoic acid; retinoic acid receptor; retinoic acid receptor alpha; transcription factor; UTX protein, human; Article; cell differentiation; cell maturation; chromatin immunoprecipitation; controlled study; flow cytometry; fluorescence activated cell sorting; gene activation; gene control; gene expression; gene overexpression; gene silencing; gene targeting; genetic transcription; genetic transfection; human; human cell; immunoprecipitation; in vivo study; promoter region; promyelocytic leukemia; protein depletion; protein interaction; quantitative analysis; retrovirus infection; reverse transcription polymerase chain reaction; transcription initiation; U937 cell line; article; drug effect; gene expression regulation; genetics; HEK293 cell line; leukemia; metabolism; pathology; tumor cell line; Antineoplastic Agents; Cell Differentiation; Cell Line, Tumor; DNA-Binding Proteins; Gene Expression Regulation, Neoplastic; Gene Knockdown Techniques; HEK293 Cells; Histone Demethylases; Histones; Humans; Leukemia; Nuclear Proteins; Promoter Regions, Genetic; Receptors, Retinoic Acid; Transcription Factors; Tretinoin; U937 Cells
Año:2014
Volumen:34
Número:19
Página de inicio:3765
Página de fin:3775
DOI: http://dx.doi.org/10.1128/MCB.00839-14
Título revista:Molecular and Cellular Biology
Título revista abreviado:Mol. Cell. Biol.
ISSN:02707306
CODEN:MCEBD
CAS:lysine, 56-87-1, 6899-06-5, 70-54-2; protein, 67254-75-5; retinoic acid, 302-79-4; histone, 9062-68-4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02707306_v34_n19_p3765_RochaViegas

Referencias:

  • Lee, M.G., Villa, R., Trojer, P., Norman, J., Yan, K.P., Reinberg, D., Di Croce, L., Shiekhattar, R., Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination (2007) Science, 318, pp. 447-450. , http://dx.doi_.org/10.1126/science.1149042
  • Agger, K., Cloos, P.A., Christensen, J., Pasini, D., Rose, S., Rappsilber, J., Issaeva, I., Helin, K., UTX and JMJD3 are histone H3K27 demethylases involved inHOXgene regulation and development (2007) Nature, 449, pp. 731-734. , http://dx.doi.org/10.1038/nature06145
  • Hong, S., Cho, Y.W., Yu, L.R., Yu, H., Veenstra, T.D., Ge, K., Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases (2007) Proc. Natl. Acad. Sci. U. S. A., 104, pp. 18439-18444. , http://dx_.doi.org/10.1073/pnas.0707292104
  • Morales Torres, C., Laugesen, A., Helin, K., Utx is required for proper induction of ectoderm and mesoderm during differentiation of embryonic stem cells (2013) PLoS One, 8, p. e60020. , http://dx.doi.org/10.1371/journal_.pone.0060020
  • Seenundun, S., Rampalli, S., Liu, Q.C., Aziz, A., Palii, C., Hong, S., Blais, A., Dilworth, F.J., UTX mediates demethylation of H3K27me3 at muscle-specific genes during myogenesis (2010) EMBO J., 29, pp. 1401-1411. , http://dx.doi.org/10.1038/emboj.2010.37
  • Liu, J., Mercher, T., Scholl, C., Brumme, K., Gilliland, D.G., Zhu, N., A functional role for the histone demethylase UTX in normal and malignant hematopoietic cells (2012) Exp. Hematol., 40, pp. 487-498.e3. , http://dx.doi.org/10_.1016/j.exphem.2012.01.017
  • Shahhoseini, M., Taghizadeh, Z., Hatami, M., Baharvand, H., Retinoic acid dependent histone 3 demethylation of the clustered HOX genes during neural differentiation of human embryonic stem cells (2013) Biochem. Cell Biol., 91, pp. 116-122. , http://dx.doi.org/10.1139/bcb-2012-0049
  • de The, H., Chen, Z., Acute promyelocytic leukaemia: novel insights into the mechanisms of cure (2010) Nat. Rev. Cancer, 10, pp. 775-783. , http://dx.doi_.org/10.1038/nrc2943
  • Di Croce, L., Chromatin modifying activity of leukaemia associated fusion proteins (2005) Hum. Mol. Genet, 14 (1), pp. R77-R84. , http://dx.doi_.org/10.1093/hmg/ddi109
  • Villa, R., Morey, L., Raker, V.A., Buschbeck, M., Gutierrez, A., De Santis, F., Corsaro, M., Di Croce, L., The methyl-CpG binding protein MBD1 is required for PML-RARalpha function (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 1400-1405. , http://dx.doi.org_/10.1073/pnas.0509343103
  • Villa, R., Pasini, D., Gutierrez, A., Morey, L., Occhionorelli, M., Vire, E., Nomdedeu, J.F., Di Croce, L., Role of the polycomb repressive complex 2 in acute promyelocytic leukemia (2007) Cancer Cell, 11, pp. 513-525. , http://dx.doi.org/10.1016/j_.ccr.2007.04.009
  • Di Croce, L., Raker, V.A., Corsaro, M., Fazi, F., Fanelli, M., Faretta, M., Fuks, F., Pelicci, P.G., Methyltransferase recruitment and DNA hypermethylation of target promoters by an oncogenic transcription factor (2002) Science, 295, pp. 1079-1082. , http://dx.doi.org/10.1126/science.1065173
  • Pandolfi, P.P., Oncogenes and tumor suppressors in the molecular pathogenesis of acute promyelocytic leukemia (2001) Hum. Mol. Genet., 10, pp. 769-775. , http://dx.doi.org/10.1093/hmg/10.7.769
  • Cho, Y.W., Hong, T., Hong, S., Guo, H., Yu, H., Kim, D., Guszczynski, T., Ge, K., PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex (2007) J. Biol. Chem., 282, pp. 20395-20406. , http://dx.doi.org/10.1074/jbc_.M701574200
  • Dou, Y., Milne, T.A., Ruthenburg, A.J., Lee, S., Lee, J.W., Verdine, G.L., Allis, C.D., Roeder, R.G., Regulation of MLL1 H3K4 methyltransferase activity by its core components (2006) Nat. Struct. Mol. Biol., 13, pp. 713-719. , http://dx.doi_.org/10.1038/nsmb1128
  • Steward, M.M., Lee, J.S., O'Donovan, A., Wyatt, M., Bernstein, B.E., Shilatifard, A., Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes (2006) Nat. Struct. Mol. Biol., 13, pp. 852-854. , http://dx_.doi.org/10.1038/nsmb1131
  • Brummelkamp, T.R., Bernards, R., Agami, R., A system for stable expression of short interfering RNAs in mammalian cells (2002) Science, 296, pp. 550-553. , http://dx.doi.org/10.1126/science.1068999
  • Lanotte, M., Martin-Thouvenin, V., Najman, S., Balerini, P., Valensi, F., Berger, R., NB4, a maturation inducible cell line with t(15;17) marker isolated from a human acute promyelocytic leukemia (M3) (1991) Blood, 77, pp. 1080-1086
  • Bijl, J.J., van Oostveen, J.W., Walboomers, J.M., Brink, A.T., Vos, W., Ossenkoppele, G.J., Meijer, C.J., Differentiation and cell-type-restricted expression of HOXC4, HOXC5 and HOXC6 in myeloid leukemias and normal myeloid cells (1998) Leukemia, 12, pp. 1724-1732. , http://dx.doi.org/10.1038/sj_.leu.2401106
  • Morey, L., Brenner, C., Fazi, F., Villa, R., Gutierrez, A., Buschbeck, M., Nervi, C., Di Croce, L., MBD3, a component of the NuRD complex, facilitates chromatin alteration and deposition of epigenetic marks (2008) Mol. Cell. Biol., 28, pp. 5912-5923. , http://dx.doi.org/10.1128_/MCB.00467-08
  • Rosenbauer, F., Tenen, D.G., Transcription factors in myeloid development: balancing differentiation with transformation (2007) Nat. Rev. Immunol., 7, pp. 105-117. , http://dx.doi.org/10.1038/nri2024
  • Yoshida, H., Ichikawa, H., Tagata, Y., Katsumoto, T., Ohnishi, K., Akao, Y., Naoe, T., Kitabayashi, I., PML-retinoic acid receptor alpha inhibits PML IV enhancement of PU (2007) 1-induced C/EBPepsilon expression in myeloid differentiation. Mol. Cell. Biol., 27, pp. 5819-5834. , http:_//dx.doi.org/10.1128/MCB.02422-06
  • Park, D.J., Vuong, P.T., de Vos, S., Douer, D., Koeffler, H.P., Comparative analysis of genes regulated by PML/RAR alpha and PLZF/RAR alpha in response to retinoic acid using oligonucleotide arrays (2003) Blood, 102, pp. 3727-3736. , http://dx.doi.org/10.1182/blood-2003-02-0412
  • Hofmann, A., Gerrits, B., Schmidt, A., Bock, T., Bausch-Fluck, D., Aebersold, R., Wollscheid, B., Proteomic cell surface phenotyping of differentiating acute myeloid leukemia cells (2010) Blood, 116, pp. e26-e34. , http://dx.doi.org_/10.1182/blood-2010-02-271270
  • Liao, J., Humphrey, S.E., Poston, S., Taparowsky, E.J., Batf promotes growth arrest and terminal differentiation of mouse myeloid leukemia cells (2011) Mol. Cancer Res., 9, pp. 350-363. , http://dx.doi.org/10.1158/1541-7786_.MCR-10-0375
  • Goo, Y.H., Sohn, Y.C., Kim, D.H., Kim, S.W., Kang, M.J., Jung, D.J., Kwak, E., Lee, J.W., Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins (2003) Mol. Cell. Biol., 23, pp. 140-149. , http://dx_.doi.org/10.1128/MCB.23.1.140-149.2003
  • Luscher-Firzlaff, J., Gawlista, I., Vervoorts, J., Kapelle, K., Braunschweig, T., Walsemann, G., Rodgarkia-Schamberger, C., Luscher, B., The human trithorax protein hASH2 functions as an oncoprotein (2008) Cancer Res., 68, pp. 749-758. , http://dx.doi.org/10.1158/0008-5472.CAN-07-3158
  • Wan, M., Liang, J., Xiong, Y., Shi, F., Zhang, Y., Lu, W., He, Q., Songyang, Z., The trithorax group protein Ash2l is essential for pluripotency and maintaining open chromatin in embryonic stem cells (2013) J. Biol. Chem., 288, pp. 5039-5048. , http://dx.doi.org/10.1074/jbc.M112.424515
  • Lee, S.K., Anzick, S.L., Choi, J.E., Bubendorf, L., Guan, X.Y., Jung, Y.K., Kallioniemi, O.P., Lee, J.W., A nuclear factor, ASC-2, as a canceramplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo (1999) J. Biol. Chem., 274, pp. 34283-34293. , http://dx.doi.org/10.1074/jbc.274.48.34283
  • Lee, S., Lee, D.K., Dou, Y., Lee, J., Lee, B., Kwak, E., Kong, Y.Y., Lee, J.W., Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 15392-15397. , http://dx.doi.org/10.1073/pnas.0607313103
  • Hong, S., Choi, H.M., Park, M.J., Kim, Y.H., Choi, Y.H., Kim, H.H., Cheong, J., Activation and interaction of ATF2 with the coactivator ASC-2 are responsive for granulocytic differentiation by retinoic acid (2004) J. Biol. Chem., 279, pp. 16996-17003. , http://dx.doi.org/10.1074/jbc.M311752200

Citas:

---------- APA ----------
Rocha-Viegas, L., Villa, R., Gutierrez, A., Iriondo, O., Shiekhattar, R. & Croce, L.D. (2014) . Role of UTX in retinoic acid receptor-mediated gene regulation in leukemia. Molecular and Cellular Biology, 34(19), 3765-3775.
http://dx.doi.org/10.1128/MCB.00839-14
---------- CHICAGO ----------
Rocha-Viegas, L., Villa, R., Gutierrez, A., Iriondo, O., Shiekhattar, R., Croce, L.D. "Role of UTX in retinoic acid receptor-mediated gene regulation in leukemia" . Molecular and Cellular Biology 34, no. 19 (2014) : 3765-3775.
http://dx.doi.org/10.1128/MCB.00839-14
---------- MLA ----------
Rocha-Viegas, L., Villa, R., Gutierrez, A., Iriondo, O., Shiekhattar, R., Croce, L.D. "Role of UTX in retinoic acid receptor-mediated gene regulation in leukemia" . Molecular and Cellular Biology, vol. 34, no. 19, 2014, pp. 3765-3775.
http://dx.doi.org/10.1128/MCB.00839-14
---------- VANCOUVER ----------
Rocha-Viegas, L., Villa, R., Gutierrez, A., Iriondo, O., Shiekhattar, R., Croce, L.D. Role of UTX in retinoic acid receptor-mediated gene regulation in leukemia. Mol. Cell. Biol. 2014;34(19):3765-3775.
http://dx.doi.org/10.1128/MCB.00839-14