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Identification of Bach2 as a B-cell-specific partner for small maf proteins that negatively regulate the immunoglobulin heavy chain gene 3′ enhancer
Open accessAbstract
Maf family transcription factors are important regulators in various differentiation systems. Putative Maf recognition elements (MAREs) are found in the 3' enhancer region of the immunoglobulin heavy chain (IgH) gene. These elements are bound in B-cell extracts by a heterodimeric protein complex containing both Bach2 and a small Maf protein. Analysis of normal hematopoietic cells revealed that Bach2 is specifically expressed in B cells. Bach2 is abundantly expressed in the early stages of B-cell differentiation and turned off in terminally differentiated cells. Bach2 acts together with MafK as a negative effector of the IgH 3' enhancer and binds to the co-repressor SMRT (silencing mediator of retinoid and thyroid receptor). Hence the Bach2-small-Maf heterodimer may represent the first example of a B-cell lineage, and of a developmental stage-restricted negative effector of the MARE in the IgH 3' enhancer region.
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“The latter protein is a small bZip transcription factor that, depending upon its heterodimeric partner, can either repress or activate gene expression (Hintze et al., 2007; Igarashi and Sun, 2006; Muto et al., 1998; Ochiai et al., 2006; Zhang et al., 2006).”
From Influence of Metabolism on Epigenetics and Disease (2013) · cites this paper as Muto et al., 1998
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Cites
Andrews, N. C., & Faller, D. V. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.9.2499 · Cited by 2,292
RAG-2-deficient mice lack mature lymphocytes owing to inability to initiate V(D)J rearrangement
Shinkai, Y. (1992) · Cell · doi:10.1016/0092-8674(92)90029-c · Cited by 2,150
Long-Term Lymphohematopoietic Reconstitution by a Single CD34-Low/Negative Hematopoietic Stem Cell
Osawa, M., Hanada, K., Hamada, H., & Nakauchi, H. (1996) · Science · doi:10.1126/science.273.5272.242 · Cited by 2,141
Self-citationKearney, J. F., Radbruch, A., Liesegang, B., & Rajewsky, K. (1979) · The Journal of Immunology · doi:10.4049/jimmunol.123.4.1548 · Cited by 1,852
Moi, P., Chan, K., Asunis, I., Cao, A., & Kan, Y. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.9926 · Cited by 1,607
Resolution and characterization of pro-B and pre-pro-B cell stages in normal mouse bone marrow.
Hardy, R. R., Carmack, C. E., Shinton, S. A., Kemp, J. D., & Hayakawa, K. (1991) · The Journal of Experimental Medicine · doi:10.1084/jem.173.5.1213 · Cited by 1,604
pEF-BOS, a powerful mammalian expression vector
Mizushima, S., & Nagata, S. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.17.5322 · Cited by 1,594
Role of the histone deacetylase complex in acute promyelocytic leukaemia
Lin, R. J., Nagy, L., Inoue, S., Shao, W., Miller, W. H., & Evans, R. M. (1998) · Nature · doi:10.1038/35895 · Cited by 1,060
Grignani, F., Matteis, S. D., Nervi, C., Tomassoni, L., Gelmetti, V., Cioce, M., Fanelli, M., Ruthardt, M., Ferrara, F. F., Zamir, I., et al. (1998) · Nature · doi:10.1038/35901 · Cited by 1,004
Association of Spindle Assembly Checkpoint Component XMAD2 with Unattached Kinetochores
Chen, R., Waters, J. C., Salmon, E. D., & Murray, A. W. (1996) · Science · doi:10.1126/science.274.5285.242 · Cited by 783
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Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630
Komatsu, M., Kurokawa, H., Waguri, S., Taguchi, K., Kobayashi, A., Ichimura, Y., Sou, Y.-S., Ueno, I., Sakamoto, A., Tong, K. I., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2021 · Cited by 2,288
“Plasmids expressing Nrf2, Keap1 and p62 wild-type or its mutants were transfected into Hepa1 cells along with pNQO1-ARE reporter plasmid and pRL-T”
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Shelef, M. A., & Calame, K. L. (2005) · Nature reviews. Immunology · doi:10.1038/nri1572 · Cited by 917
Kobayashi, M., & Yamamoto, M. P. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.007 · Cited by 862
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Hemoprotein Bach1 regulates enhancer availability of heme oxygenase‐1 gene
Sun, J., Hoshino, H., Takaku, K., Nakajima, O., Muto, A., Suzuki, H., Tashiro, S., Takahashi, S., Shibahara, S., Alam, J., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf516 · Cited by 637
Self-citationOgawa, K., Sun, J., Taketani, S., Nakajima, O., Nishitani, C., Sassa, S., Hayashi, N., Yamamoto, M., Shibahara, S., Fujita, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2835 · Cited by 532
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Dodson, M. B., de la Vega, M. R., Cholanians, A. B., Schmidlin, C. J., Chapman, E., & Zhang, D. D. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021856 · Cited by 540
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Motohashi, H., O'Connor, T., Katsuoka, F., Engel, J. D., & Yamamoto, M. P. (2002) · Gene · doi:10.1016/s0378-1119(02)00788-6 · Cited by 456
Self-citationKao, H., Downes, M., Ordentlich, P., & Evans, R. M. (2000) · Genes & Development · doi:10.1101/gad.14.1.55 · Cited by 424
“…and Pbx1 have been demonstrated (Dhordain et al. 1997; Hong et al. 1997; He et al. 1998; Huynh and Bardwell 1998; Kao et al. 1998; Lin et al. 1998; Muto et al. 1998; Wong and Privalsky 1998; Asahara et al. 1999; Bailey et al. 1999), suggesting that corepressors, like coactivators, may function as…”
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“BACH2 is highly expressed on B cells, suppresses the production of immunoglobulins [98], and has a known immune function as a regulator of nucleic acid-triggered antiviral responses in human cells [99].”
BackgroundMolecular Basis of Electrophilic and Oxidative Defense: Promises and Perils of Nrf2
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Muto, A., Tashiro, S., Nakajima, O., Hoshino, H., Takahashi, S., Sakoda, E., Ikebe, D., Yamamoto, M. P., & Igarashi, K. (2004) · Nature · doi:10.1038/nature02596 · Cited by 292
“Bach2 is a B-cell-specific transcription repressor interacting with the small Maf proteins whose expression is high only before the plasma cell stag”
BackgroundSelf-citationPlasma cell development and survival
Oracki, S. A., Walker, J. A., Hibbs, M. L., Corcoran, L. M., & Tarlinton, D. M. (2010) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00940.x · Cited by 291
Heme Oxygenase-1 and the Vascular Bed: From Molecular Mechanisms to Therapeutic Opportunities
Łoboda, A., Jaźwa, A., Grochot‐Przeczek, A., Rutkowski, A. J., Cisowski, J., Agarwal, A., Józkowicz, A., & Dulak, J. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2043 · Cited by 265
“Moreover, another related transcription repressor, Bach2, has been discovered to be expressed in the brain (323) and B lymphocytes (301); however, no data are available regarding the role of Bach2 in endothelial cells.”
Small Maf proteins (MafF, MafG, MafK): History, structure and function
Katsuoka, F., & Yamamoto, M. P. (2016) · Gene · doi:10.1016/j.gene.2016.03.058 · Cited by 253
“Similarly, Bach2-sMaf heterodimers are known to negatively regulate the immunoglobulin heavy chain gene through the 3’ enhancer regions of MAREs (Muto et al., 1998).”
Self-citationThe Heme-Bach1 Pathway in the Regulation of Oxidative Stress Response and Erythroid Differentiation
Igarashi, K., & Sun, J. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.107 · Cited by 248
Self-citationThe genetic network controlling plasma cell differentiation
Nutt, S. L., Taubenheim, N., Hasbold, J., Corcoran, L. M., & Hodgkin, P. D. (2011) · Seminars in Immunology · doi:10.1016/j.smim.2011.08.010 · Cited by 224
Roles of Nrf2 in cell proliferation and differentiation
Murakami, S., & Motohashi, H. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.030 · Cited by 226
Medici, M., Porcu, E., Pistis, G., Teumer, A., Brown, S. J., Jensen, R. A., Rawal, R., Roef, G. L., Plantinga, T. S., Vermeulen, S. H., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004123 · Cited by 218
“BACH2 is specifically expressed in early stages of B-cell differentiation and represses different immunoglobulin genes [56].”
Pinaud, E., Khamlichi, A. A., Morvan, C. L., Drouet, M., Nalesso, V., Bert, M. L., & Cogné, M. (2001) · Immunity · doi:10.1016/s1074-7613(01)00181-9 · Cited by 218
“…Caroline Le Morvan,1 Mireille Drouet,1 Valérie Nalesso,2 Marc Le Bert,2 and Michel Cogné1,3 1Laboratoire d’Immunologie proteins, which altogether may either mediate repres-CNRS UMR6101 sion of the 3 elements in lymphocytes or activation inFaculté de Médecine plasma cells (Muto et al., 1998).”
BackgroundBach2 represses plasma cell gene regulatory network in B cells to promote antibody class switch
Muto, A., Ochiai, K., Kimura, Y., Itoh‐Nakadai, A., Calame, K. L., Ikebe, D., Tashiro, S., & Igarashi, K. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.257 · Cited by 226
“Bach2 is a B-cell-specific transcription factor (Oyake et al, 1996; Muto et al, 1998).”
BackgroundSelf-citationCritical Residues within the BTB Domain of PLZF and Bcl-6 Modulate Interaction with Corepressors
Melnick, A. M., Carlile, G. W., Ahmad, K. F., Kiang, C. L., Corcoran, C. M., Bardwell, V. J., Privé, G. G., & Licht, J. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.6.1804-1818.2002 · Cited by 209
“Most BTB domains possess the conserved charged pocket; therefore, it is not surprising that many other BTB transcription factors bind to corepressors, including Bach-2, GAGA, and ZID (23, 38).”
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Zgórzyńska, E., Dziedzic, B., & Walczewska, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179592 · Cited by 215
“Such downregulation has been demonstrated for heme oxygenase-1 (HO-1) [68,69], NAD(P)H:quinone dehydrogenase 1 (NQO1) [70] and immunoglobulin heavy chain gene 3‘ enhancer [71].”
BackgroundNili, E., Cojocaru, G., Kalma, Y., Ginsberg, D., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Berger, R., Shaklai, S., Amariglio, N., et al. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.18.3297 · Cited by 193
Methionine adenosyltransferase II serves as a transcriptional corepressor of Maf oncoprotein
Katoh, Y., Ikura, T., Hoshikawa, Y., Tashiro, S., Ito, T., Ohta, M., Kera, Y., Noda, T., & Igarashi, K. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.018 · Cited by 185
Self-citationBach2 maintains T cells in a naive state by suppressing effector memory-related genes
Tsukumo, S.-I., Unno, M., Muto, A., Takeuchi, A., Kometani, K., Kurosaki, T., Igarashi, K., & Saito, T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306691110 · Cited by 168
“Although we initially reported that Bach2 was mainly expressed in B cells (17), we found now that it is also expressed in T cells and at levels almost compatible to B cells whereas nonT/B cells express a much lower level (Fig.”
BackgroundSelf-citationTargeting the Nrf2 pathway against cardiovascular disease
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“In contrast to NF-E2, Bach proteins function as transcriptional repressors [16,18,19].”
BackgroundPlasmacytic Transcription Factor Blimp-1 Is Repressed by Bach2 in B Cells
Ochiai, K., Katoh, Y., Ikura, T., Hoshikawa, Y., Noda, T., Karasuyama, H., Tashiro, S., Muto, A., & Igarashi, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607592200 · Cited by 162
Self-citationDual roles of NRF2 in tumor prevention and progression: Possible implications in cancer treatment
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The diverse roles of IRF4 in late germinal center B‐cell differentiation
Silva, N. S. D., Simonetti, G., Heise, N., & Klein, U. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01113.x · Cited by 154
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Simmonds, M. J. (2013) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.56 · Cited by 132
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“…well as two distantly related proteins termed Bach1 and Bach2 (Chan et al., 1993a, 1993b; Moi et al., 1994; Itoh et al., 1995; Oyake et al., 1996; Muto et al., 1998; Kobayashi Received 16 July 2010; revised 8 September 2010; accepted 18 September 2010; published online 8 November 2010…”
Nakamura, A., Ebina‐Shibuya, R., Itoh‐Nakadai, A., Muto, A., Shima, H., Saigusa, D., Aoki, J., Ebina, M., Nukiwa, T., & Igarashi, K. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20130028 · Cited by 123
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BackgroundSelf-citationCooperative transcriptional repression by BCL6 and BACH2 in germinal center B-cell differentiation
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“BACH2 binds DNA consensus sequences, termed MARE motifs (59TGAG/CTCA39), by forming a heterodimer with small leucine zipper MAF proteins such as MAFK, MAFG, and MAFF.(22,23) The importance of Bach2 for mature B cells was revealed in Bach2deficent mice (Bach2), which is similar to Bcl6mice, display a loss of GCs, and a…”
BackgroundInfluentialRegulation of the plasma cell transcription factor Blimp-1 gene by Bach2 and Bcl6
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Self-citationKobayashi, A., Yamagiwa, H., Hoshino, H., Muto, A., Sato, K., Morita, M., Hayashi, N., Yamamoto, M. P., & Igarashi, K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1733-1746.2000 · Cited by 112
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“Cotransfection of pEF-SP ( 13 ) did not interfere with the activity of our reporter constructs.”
BackgroundSelf-citationIgarashi, K., & Watanabe‐Matsui, M. (2014) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.232.229 · Cited by 115
“While the expression of Bach2 is considered to be rather specific to B cells and neurons (Muto et al. 1998; Hoshino and Igarashi 2002), recent studies have established that Bach2 is also expressed in T cells (Roychoudhuri et al. 2013; Tsukumo et al. 2013).”
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Self-citationDeltour, S., Guérardel, C., & Leprince, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14831 · Cited by 108
The 3′ IgH regulatory region: A complex structure in a search for a function
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Hoshino, H., Kobayashi, A., Yoshida, M., Kudo, N. R., Oyake, T., Motohashi, H., Hayashi, N., Yamamoto, M. P., & Igarashi, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15370 · Cited by 106
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Yoshida, C., Tokumasu, F., Hohmura, K. I., Bungert, J., Hayashi, N., Nagasawa, T., Engel, J. D., Yamamoto, M. P., Takeyasu, K., & Igarashi, K. (1999) · Genes to Cells · doi:10.1046/j.1365-2443.1999.00291.x · Cited by 96
Self-citationGenetic determination of the hypothalamic–pituitary–thyroid axis: where do we stand?
Medici, M., Visser, W. E., Visser, T. J., & Peeters, R. P. (2015) · Endocrine Reviews · doi:10.1210/er.2014-1081 · Cited by 92
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BackgroundOrchestration of plasma cell differentiation by Bach2 and its gene regulatory network
Igarashi, K., Ochiai, K., Itoh‐Nakadai, A., & Muto, A. (2014) · Immunological Reviews · doi:10.1111/imr.12201 · Cited by 93
Self-citationMuto, A., Tashiro, S., Tsuchiya, H., Kume, A., Kanno, M., Ito, E., Yamamoto, M. P., & Igarashi, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112003200 · Cited by 92
Self-citationIgarashi, K., Nishizawa, H., Saiki, Y., & Matsumoto, M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101032 · Cited by 89
Self-citationTranscription Factor Effector Domains
Frietze, S. E., & Farnham, P. (2011) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-9069-0_12 · Cited by 93
Kaneko, K., Furuyama, K., Fujiwara, T., Kobayashi, R., Ishida, H., Harigae, H., & Shibahara, S. (2013) · Haematologica · doi:10.3324/haematol.2013.085449 · Cited by 83
Tanaka, H., Muto, A., Shima, H., Katoh, Y., Sax, N., Tajima, S., Brydun, A., Ikura, T., Yoshizawa-Sugata, N., Masai, H., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.713842 · Cited by 80
“Bach2 is expressed in B cells from pro-B to mature-B cell stages but not in plasma cells, showing a pattern totally opposite that of Blimp-1 (15, 17).”
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Kataoka, K., Yoshitomo-Nakagawa, K., Shioda, S., & Nishizawa, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007643200 · Cited by 73
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Sasaki, S., Ito, E., Toki, T., Maekawa, T., Kanezaki, R., Umenai, T., Muto, A., Nagai, H., Kinoshita, T., Yamamoto, M. P., et al. (2000) · Oncogene · doi:10.1038/sj.onc.1203716 · Cited by 69
“In the mouse, Bach2 is expressed in pro-B, pre-B, immature B and mature B cell lines, and it is absent in plasmacytoma cell lines (Muto et al., 1998).”
BackgroundMethodSelf-citationTiedemann, R. E., Mao, X., Shi, C., Zhu, Y. X., Palmer, S. E., Sébag, M., Marler, R., Chesi, M., Fonseca, R., Bergsagel, P. L., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34149 · Cited by 66
Microarray‐based understanding of normal and malignant plasma cells
Vos, J. D., Hose, D., Reme, T. X., Tarte, K., Moreaux, J., Mahtouk, K., Jourdan, M., Goldschmidt, H., Rossi, J., Cremer, F. W., et al. (2006) · Immunological Reviews · doi:10.1111/j.0105-2896.2006.00362.x · Cited by 65
“According to this model, translocation t(11;14), hyperdiploid, and non-hyperdiploid karyotypes, each defines a distinct subgroup of the disease.”
BackgroundMethodInfluentialCharacterization of the Murine mafF Gene
Onodera, K., Shavit, J. A., Motohashi, H., Katsuoka, F., Akasaka, J.-E., Engel, J. D., & Yamamoto, M. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21162 · Cited by 63
Self-citationVeraksa, A. N., McGinnis, N., Li, X., Mohler, J., & McGinnis, W. J. (2000) · Development · doi:10.1242/dev.127.18.4023 · Cited by 61
Bach2 Controls T Follicular Helper Cells by Direct Repression of Bcl-6
Lahmann, A., Kuhrau, J., Fuhrmann, F., Heinrich, F., Bauer, L., Durek, P., Mashreghi, M., & Hutloff, A. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1801400 · Cited by 60
“Bach2 is known to bind to AP-1 motifs (10), and bioinformatic analysis revealed that this region contains several potential Bach2 binding sites (Fig.”
BackgroundIgarashi, K., Ochiai, K., & Muto, A. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm106 · Cited by 58
Self-citationYoshida, C., Yoshida, F., Sears, D., Hart, S., Ikebe, D., Muto, A., Basu, S., Igarashi, K., & Melo, J. V. (2006) · Blood · doi:10.1182/blood-2005-12-040972 · Cited by 60
Self-citationCannabinoid Receptor 2-Centric Molecular Feedback Loop Drives Necroptosis in Diabetic Heart Injuries
Gao, P., Cao, M., Jiang, X., Wang, X., Zhang, G., Tang, X., Yang, C., Komuro, I., Ge, J., Li, L., et al. (2022) · Circulation · doi:10.1161/circulationaha.122.059304 · Cited by 56
B-cell–specific transcription factor BACH2 modifies the cytotoxic effects of anticancer drugs
Kamio, T., Toki, T., Kanezaki, R., Sasaki, S., Tandai, S., Terui, K., Ikebe, D., Igarashi, K., & Ito, E. (2003) · Blood · doi:10.1182/blood-2002-12-3656 · Cited by 55
Self-citationOmura, S., Suzuki, H., Toyofuku, M., Ozono, R., Kohno, N., & Igarashi, K. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00832.x · Cited by 55
“Ten micrograms of whole cell extracts, prepared from macrophages or SMC as previously described (Muto et al. 1998) and processed for immunoblotting using antisera against HO-1 (kind gift from Prof Shigeru Taketani, Kyoto Institute of Technology, Japan) and MafK (Igarashi et al. 1995).”
MethodSelf-citationZhang, Z., Leir, S., & Harris, A. (2014) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2014-0263oc · Cited by 54
Repression of an Interleukin-4-responsive Promoter Requires Cooperative BCL-6 Function
Harris, M. B., Mostecki, J. W., & Rothman, P. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412649200 · Cited by 54
A peptide aptamer to antagonize BCL-6 function
Chattopadhyay, A., Tate, S., Beswick, R. W., Wagner, S. D., & Ferrigno, P. K. (2005) · Oncogene · doi:10.1038/sj.onc.1209252 · Cited by 52
Bender, D., & Hildt, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184659 · Cited by 56
“Other members of the bZIP protein family are NF-E2 (nuclear factor erythoid 2) p45 [41,42], Nrf1 (NF-E2 related factor 1) [42,43], Nrf3 [42,44,45], Bach1 (BTB (Broad-complex, Tramtrack and Bric-à-brac) and CNC homology 1) [42,46] and Bach2 (BTB and CNC homology 2) [42,47].”
BackgroundRepression of PML Nuclear Body-Associated Transcription by Oxidative Stress-Activated Bach2
Tashiro, S., Muto, A., Tanimoto, K., Tsuchiya, H., Suzuki, H., Hoshino, H., Yoshida, M., Walter, J. K., & Igarashi, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3473-3484.2004 · Cited by 51
Self-citationZhang, Y., & Hayes, J. D. (2013) · Scientific Reports · doi:10.1038/srep02006 · Cited by 45
Recognition of BACH1 quaternary structure degrons by two F-box proteins under oxidative stress
Cao, S., Garcia, S. F., Shi, H., James, E. I., Kito, Y., Shi, H., Mao, H., Kaisari, S., Róna, G., Deng, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.10.012 · Cited by 47
Transgenic expression of BACH1 transcription factor results in megakaryocytic impairment
Toki, T. (2004) · Blood · doi:10.1182/blood-2004-07-2826 · Cited by 45
Ravoet, M., Sibille, C., Roufosse, F. E., Duvillier, H., Sotiriou, C., Schandené, L., Martiat, P., Goldman, M., & Willard-Gallo, K. E. (2005) · PubMed · Cited by 45
Extended exome sequencing identifies BACH2 as a novel major risk locus for Addison's disease
Eriksson, D., Bianchi, M., Landegren, N., Nordin, J., Dalin, F., Mathioudaki, A., Eriksson, G., Hultin‐Rosenberg, L., Dahlqvist, J., Zetterqvist, H., et al. (2016) · Journal of Internal Medicine · doi:10.1111/joim.12569 · Cited by 45
Yamasaki, C. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi031 · Cited by 41
The MTG proteins: chromatin repression players with a passion for networking
Rossetti, S., Hoogeveen, A. T., & Sacchi, N. (2004) · Genomics · doi:10.1016/j.ygeno.2004.02.011 · Cited by 41
Yin Yang 1 Is a Lipopolysaccharide-Inducible Activator of the Murine 3′ Igh Enhancer, hs3
Gordon, S. J., Saleque, S., & Birshtein, B. K. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.11.5549 · Cited by 40
“of hs3 and potentially other 3 Igh enhancers (18).”
BackgroundTranscription factor BACH2 is transcriptionally regulated by the BCR/ABL oncogene
Vieira, S., Deininger, M. W., Sorour, A., Sinclair, P. B., Foroni, L., Goldman, J. M., & Melo, J. V. (2001) · Genes Chromosomes and Cancer · doi:10.1002/gcc.1200 · Cited by 40
“Since Bach2 seems to function predominantly as a transcriptional repressor (Muto et al., 1998), it is possible that inefficient expression of this factor in CML and Ph-positive ALL cells contributes to their malignant phenotype through abnormal regulation of one or more target genes.”
BackgroundResultInfluentialHeme binds to an intrinsically disordered region of Bach2 and alters its conformation
Watanabe‐Matsui, M., Matsumoto, T., Matsui, T., Ikeda‐Saito, M., Muto, A., Murayama, K., & Igarashi, K. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.11.005 · Cited by 39
Self-citationChen, Z., Pittman, E. F., Romaguera, J. E., Fayad, L., Wang, M. L., Neelapu, S. S., McLaughlin, P. J., Kwak, L. W., & McCarty, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069126 · Cited by 39
Pointud, J., Larsson, J., Dastugue, B., & Couderc, J. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0358 · Cited by 39
“Interestingly, the combi- ation of MAZR and Bach2 potentiates this transcriptional ctivation while Bach2 alone is a transcriptional repressor Muto et al., 1998; Kobayashi et al., 2000).”
BackgroundHwang, R., Tiwari, A. K., Zai, C. C. H., Felsky, D., Remington, E., Wallace, T., Tong, R. P., de Souza, R. P., Oh, G., Potkin, S. G., et al. (2011) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2011.11.018 · Cited by 38
Type I interferons as key players in pancreatic β-cell dysfunction in type 1 diabetes
Marroquí, L., Perez-Serna, A. A., Babiloni-Chust, I., & dos Santos, R. S. (2021) · International review of cytology · doi:10.1016/bs.ircmb.2021.02.011 · Cited by 37
BACH2–BCL6 balance regulates selection at the pre-B cell receptor checkpoint
Swaminathan, S., Duy, C., & Müschen, M. (2013) · Trends in Immunology · doi:10.1016/j.it.2013.11.002 · Cited by 39
Lead, Chemical Porphyria, and Heme as a Biological Mediator.
Fujita, H., Nishitani, C., & OGAWA, K. (2002) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.196.53 · Cited by 34
“Like NF-E2 family proteins,transcription factors Bach1 and Bach2,which are basic leucine zipper(bZip) proteins,form heterodimers with the Maf proteins to bind MAREs,functioning primarily as repressors(Oyake et al.1996;Igarashi et al. 1998;Muto et al.1998;Yoshida et al.1999; Kobayashi et al.2000).”
BackgroundMahendra, A., Yang, X., Abnouf, S., Adolacion, J. R. T., Park, D., Soomro, S., Roszik, J., Coarfa, C., Romain, G., Wanzeck, K. C., et al. (2018) · Arthritis & Rheumatology · doi:10.1002/art.40772 · Cited by 33
“larly, the small macrophageactivating factor family of transcription factors (MAFF and MAFG), which have a direct impact on Ig secretion (27), were enriched in these RACCP B cells (Figure 2E).”
BackgroundNAC1, a POZ/BTB protein that functions as a corepressor
Korutla, L., Wang, P., Jackson, T. G., & Mackler, S. A. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.12.008 · Cited by 33
Kimura, T., Ivell, R., Rust, W., Mizumoto, Y., Ogita, K., Kusui, C., Matsumura, Y., Azuma, C., & Murata, Y. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1487 · Cited by 33
Chauveau, C., Jansson, E. Å., Müller, S., Cogné, M., & Pettersson, S. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.9.4637 · Cited by 33
“Bach2 is exclusively expressed at early stages of B cell differentiation and has been suggested to act as a repressor on the IgH 39 enhancer region ( 25 ).”
Background
Metadata
- Authors
- Muto, A., Hoshino, H., Madisen, L., Yanai, N., Obinata, M., Karasuyama, H., Hayashi, N., Nakauchi, H., Yamamoto, M., Groudine, M., & Igarashi, K.
- Affiliations
- University of Tsukuba (JP)
- Fred Hutch Cancer Center (US)
- Tohoku University (JP)
- Tokyo Metropolitan Institute of Medical Science (JP)
- Corresponding author
- Igarashi, Kazuhiko
- Venue
- The EMBO Journal
- Published
- 1998-10-01
- Volume
- 17
- Issue
- 19
- Pages
- 5734-5743
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1170901
- OpenAlex
- W2106931266
- Cited by
- 190
- References
- 71
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 5 · 2023: 3 · 2022: 6 · 2021: 4 · 2020: 5 · 2019: 5 · 2018: 6 · 2017: 2 · 2016: 9 · 2015: 6 · 2014: 10 · 2013: 17 · 2012: 8
- FWCI
- 2.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Naito Foundation
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- BACH2, MafK, immunoglobulin heavy chain genes, 3' enhancer, B cell differentiation, transcriptional repression, heterodimeric transcription factors
- MeSH terms
- B-Lymphocytes, Cell Differentiation, Cell Line, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Genes, Immunoglobulin, Hematopoietic Stem Cells, Immunoglobulin Heavy Chains, Nuclear Proteins, Proto-Oncogene Proteins, Transcription Factors, Leucine Zippers, Response Elements, Basic-Leucine Zipper Transcription Factors, MafK Transcription Factor, Proto-Oncogene Proteins c-maf
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