Cited by 373Hemoglobinopathies and Related DisordersHemoglobin structure and functionGenomics and Chromatin Dynamics

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Transcription factors LRF and BCL11A independently repress expression of fetal hemoglobin

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Masuda, Takeshi, Wang, Xin, Maeda, Manami, Canver, Matthew C., Sher, Falak, Funnell, Alister P. W., Fisher, Chris, Suciu, Maria, Martyn, Gabriella E., Norton, Laura J., Zhu, Catherine, Kurita, Ryo, Nakamura, Yukio, Xu, Jian, Higgs, Douglas R., Crossley, Merlin, Bauer, Daniel E., Orkin, Stuart H., Kharchenko, Peter V., Maeda, Takahiro·2016·Science

DOI 10.1126/science.aad3312PMC PMC4778394

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Abstract

Reactivating the fetal globin gene: Mutation of adult-type globin genes causes sickle cell disease and thalassemia. Although treating these hemoglobinopathies with gene therapy is possible, there is a pressing need for pharmacologic approaches to treat general patient populations. One promising approach is to reactivate repressed expression of fetal-type hemoglobin (HbF) in adult erythroid cells. Masuda et al. reveal a molecular mechanism governing HbF repression as mediated by the LRF/ZBTB7A transcription factor. The study may encourage the development of new HbF reactivation therapies for hemoglobinopathies. Science , this issue p. 285

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Fitting a mixture model by expectation maximization to discover motifs in biopolymers.
Bailey, T. L., & Elkan, C. (1994) · PubMed · Cited by 4,982
In-gel digestion for mass spectrometric characterization of proteins and proteomes
Shevchenko, A., Tomas, H., Havli, J., Olsen, J. V., & Mann, M. (2006) · Nature Protocols · doi:10.1038/nprot.2006.468 · Cited by 4,947
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Background
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BackgroundSelf-citation
Zbtb46-Dependent Altered Developmental Program in Embryonic Stem Cell-Derived Blood Cell Progenitors
Botó, P., Gerzsenyi, T. B., Lengyel, A., Szunyog, B., & Szatmári, I. (2021) · Stem Cells · doi:10.1002/stem.3424 · Cited by 3
“For example, Lrf deficiency causes lethal anemia in mouse embryo and this protein has a critical role on the repression of the fetal beta-globin gene.(15,16) Notably, repressive functions of Zbtb46 have also been documented.”
Background
TR4 and BCL11A repress γ-globin transcription via independent mechanisms
Wang, Y., Myers, G., Yu, L., Deng, K., Balbin-Cuesta, G., Singh, S. A., Guan, Y., Khoriaty, R. N., & Engel, J. D. (2024) · Blood · doi:10.1182/blood.2024024599 · Cited by 5
ZNF410 uniquely activates the NuRD component CHD4 to silence fetal hemoglobin expressionPreprint
Lan, X., Ren, R., Feng, R., Ly, L. C., Lan, Y., Zhang, Z., Aboreden, N. G., Qin, K., Horton, J. R., Grevet, J. D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.31.274324 · Cited by 4
Self-citation
Discovery of A Small Molecule non-IMiD Degrader of ZBTB7A for the Treatment of β-hemoglobinopathiesPreprint
Liu, J., Shen, Z., Park, S., Dong, Y., Yu, N., Zeng, J., Lee, H., Pate, B., Adamia, S., Vanuytsel, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.17.676148 · Cited by 4
Self-citation
Cis- and trans-acting expression quantitative trait loci differentially regulate gamma-globin gene expression
Shaikho, E. M., Farrell, J. J., Chui, D. H. K., Sebastiani, P., & Steinberg, M. H. (2018) · doi:10.1101/304899 · Cited by 5
“These genes were selected because of their role or putative role as modulators of HBG expression, except for BCL2L1 which was selected based on our HBG1 co-expression and upstream regulators analysis (Jiang et al. 2006; Zhou et al. 2010; Masuda et al. 2016; Dai et al. 2017).”
Quantification of human embryonic ζ-globin chains in Southeast Asian deletion (--SEA) carriers
Ye, Y.-H., Sun, G., Ren, Z., Liang, Y.-M., Luo, H., Lin, P., Wang, X., Dong, Z., Huang, L., Qin, L., et al. (2022) · Journal of Clinical Pathology · doi:10.1136/jcp-2022-208159 · Cited by 3
Self-citation
Effect of the LSD1 inhibitor RN-1 on γ-globin and global gene expression during erythroid differentiation in baboons (Papio anubis)
Ibañez, V., Vaitkus, K., Ruiz, M. A., Lei, Z., Maienschein‐Cline, M., Arbieva, Z. H., & Lavelle, D. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289860 · Cited by 4
The role of miR-129-5p in regulating γ-globin expression and erythropoiesis in β-thalassemia
li, J., Chen, M., Zhao, W., Lv, A., Lin, S., Zheng, Y., Cai, M., Lin, N., Xu, L., & Huang, H. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae180 · Cited by 3
Direct and indirect regulation of fetal globin transcript by the RNA-binding protein IGF2BP1
Coyne, S. M., Hwang, G.-H., Wu, T., Hossain, M. A., Vinjamur, D. S., Starrs, M. M., Zeng, J., Andresen, F., Gutierrez, A. M., Shimamura, A., et al. (2026) · Blood · doi:10.1182/blood.2025031840 · Cited by 4
Self-citation
Comprehensive regulation of γ-globin expression by epigenetic modifications and protein post-translational modifications
Ye, D., Chen, M., Zhu, Y. J., Feng, X., Xu, L., & Huang, H. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01962-5 · Cited by 4
“Inhibiting BCL11A or ZBTB7A can increase the expression of the γ-globin gene [85–87].”
p27Kip1 regulates γ-globin production
Balbin-Cuesta, G., Drysdale, C. M., Kerpet, C., Yu, L., Myers, G., Lin, Z., McGee, B. M., Friedman, A. D., Liu, X., Singh, S. A., et al. (2025) · Blood · doi:10.1182/blood.2025028895 · Cited by 3
An optimized CRISPR-Cas12a genome-wide screen reveals PTPA phosphatase pathway in fetal hemoglobin silencing
Traxler, E. A., Hotan, Q., Shao, Y., Komar, C. A., Chen, Q., Saari, M. S., Thrasher, A. J., Yang, S., Qin, K., Wang, M. Y., et al. (2026) · Blood · doi:10.1182/blood.2025030137 · Cited by 3
Applications of genome editing technologies in the treatment of human diseases
Alshorman, J., Mehran, M. J., Tembo, K. M., Mostafavi, N., Bolideei, M., & Wang, Y. L. (2026) · Gene Therapy · doi:10.1038/s41434-026-00627-z · Cited by 3
miR-365-3p mediates BCL11A and SOX6 erythroid-specific coregulation: A new player in HbF activation
Simbula, M., Manchinu, M. F., Mingoia, M., Pala, M., Asunis, I., Caria, C. A., Perseu, L., Shah, M., Crossley, M., Moi, P., et al. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.09.002 · Cited by 3
“However, these cells tend to have high background levels of HbF. 71 Insummary,miRNAsequencingoffetalliver murinecellsshowedthat miR-365-3p is overexpressed in BCL11A -null mice.”
BackgroundSelf-citation
Creating New Cis-Regulatory Elements of HBD to Reactivate Delta-Globin
Chen, L., Liu, D., Hong, W., Xu, L., Cheng, L., Luo, Y., Xu, H. M., Li, X., Fang, J., & Li, X. (2025) · Human Gene Therapy · doi:10.1089/hum.2024.186 · Cited by 3
The histone deacetylase inhibitor CT-101 flips the switch to fetal hemoglobin expression in sickle cell disease mice
Takezaki, M., Li, Y., Xu, H., Patel, N., Lucas, R., Cerbone, R. E., Koti, S., Hendrick, C. L., Junker, L. H., & Pace, B. S. (2025) · PLoS ONE · doi:10.1371/journal.pone.0323550 · Cited by 3
Beyond transfusions and transplants: genomic innovations rewriting the narrative of thalassemia
Shi, L., Yan, X., Xia, Y., Zhao, Y., Zhu, X., Li, Q., & Xu, Z. (2025) · Annals of Hematology · doi:10.1007/s00277-025-06548-y · Cited by 6
“ZBTB7A/LRF represses γ-globin via a BCL11A-independent NuRD complex [103 , 104], while KLF1 promotes β-globin expression and suppresses γ-globin by activating BCL11A/LRF [105].”
The future of academic haematology
Hay, D., Hatton, C. S. R., & Weatherall, D. J. (2016) · British Journal of Haematology · doi:10.1111/bjh.14472 · Cited by 3
Surface plasmon resonance based analysis of the binding of LYAR protein to the rs368698783 (G>A) polymorphic Aγ-globin gene sequences mutated in β-thalassemia
Gemmo, C., Breveglieri, G., Marzaro, G., Lampronti, I., Cosenza, L. C., Gasparello, J., Zuccato, C., Fabbri, E., Borgatti, M., Chilin, A., et al. (2019) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-01987-9 · Cited by 3
Multi-Locus Models to Address Hb F Variability in Portuguese β-Thalassemia Carriers
Manco, L., Bento, C., Relvas, L., Cunha, E., Pereira, J., Moreira, V., Álvarez, M., Maia, T. M., & Ribeiro, M. L. (2020) · Hemoglobin · doi:10.1080/03630269.2020.1753766 · Cited by 3
“BCL11A does not interact directly with the c-globin promoter but targets intergenic region(s), the LCR, and sequences between HBG1 and HBD [13].”
Background
Targeting ZNF410 as a potential β-hemoglobinopathy therapy
Tumburu, L., & Thein, S. L. (2021) · Nature Genetics · doi:10.1038/s41588-021-00817-y · Cited by 3
ZBTB7A regulates primed‐to‐naïve transition of pluripotent stem cells via recognition of the PNT‐associated sequence by zinc fingers 1–2 and recognition of γ‐globin −200 gene element by zinc fingers 1–4
Yang, Y., Xiao, L., Xue, Y., Idris, M. O., Liu, J., Pei, D., Shi, Y., Liao, B., & Li, F. (2023) · FEBS Journal · doi:10.1111/febs.16789 · Cited by 3
Activation of γ-globin expression by LncRNA-mediated ERF promoter hypermethylation in β-thalassemia
Bao, X., Gao, Y., Wang, Z., Ye, Y., Chen, D., Zuo, Y., Zhao, C., & Xu, X. (2024) · Clinical Epigenetics · doi:10.1186/s13148-023-01614-6 · Cited by 3
“Several modulators, such as transcription factors (TFs) BCL11A and LRF, have been uncovered to regulate HbF expression by directly binding to γ-globin promoter [1, 2].”
Background
A common TBP-binding site mutation elevates fetal hemoglobin levels by competitive globin switching change in β-thalassemia
Song, M., Wei, X., Luo, H., Wang, J., Ye, Y., Qin, L., Niu, C., Long, Y., Wang, X., Shao, C., et al. (2025) · Blood Advances · doi:10.1182/bloodadvances.2024013695 · Cited by 3
“11 Collectively, BCL11A and ZBTB7A are responsible for most γ -globin gene silencing.”
Self-citation
Genome Editing of Erythroid Cell Culture Model Systems
Yik, J. J., Crossley, M., & Quinlan, K. G. R. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7428-3_15 · Cited by 2
Self-citation
The BTB transcription factors ZBTB11 and ZFP131 maintain pluripotency by pausing POL II at pro-differentiation genesPreprint
Garipler, G., Lu, C., Morrissey, A., López-Zepeda, L. S., Vidal, S. E., Aydın, B., Stadtfeld, M., Ohler, U., Mahony, S., Sanjana, N. E., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.23.391771 · Cited by 3
“ZBTB TFs are also known to interact with the subunits of histone deacetylase complexes (David et al., 1998; Maeda, 2016; Masuda et al., 2016).”
Background
Reactivation of developmentally silenced globin genes through genomic deletions reveals that enhancer distance mattersPreprint
Felder, A.-K., Tjalsma, S. J. D., Verhagen, H. J. M. P., Majied, R., Verstegen, M. J. A. M., Verheul, T. C. J., Mohnani, R., Gremmen, R., Krijger, P. H. L., Philipsen, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.13.632719 · Cited by 3
The BCL11A transcription factor stimulates the enzymatic activities of the OGG1 DNA glycosylase
Petrachkova, T., Солдаткина, О. И., Leduy, L., & Nepveu, A. (2024) · Biological Chemistry · doi:10.1515/hsz-2024-0088 · Cited by 2
MYB represses ζ-globin expression through upregulating ETO2
Dong, Z., Ye, Y., Zhang, W., Luo, H., Li, J., Zhang, Q., Zhang, X., Guo, X., & Xu, X. (2024) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2024239 · Cited by 2
“For CRISPR editing in HUDEP - 2 and CD34 + HSPCs, sgRNAs were synthesized by GenScript as previously described [10,23].”
A one-base therapeutic insertion in the HBG2 distal promoter reactivates γ-globin expression
Bao, X., Gao, Y., Chen, X., Wang, Z., Feng, X., Wang, L., Du, J., Ye, Y., Chen, F., Du, L., et al. (2025) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00626-7 · Cited by 2
“In recent years, an increasing number of HbF regulatory factors have been discovered [4–11], among which transcription factors (TFs) represented by BCL11A and LRF/ZBTB7A are known to repress the expression of γ-globin through binding to cis -acting elements in γ-globin promoter [6, 12].”
The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex
Dan-Dukor, G., Shang, S., Leighton, G. O., Travis, C. R., Schwochert, T. D., Agrawal, P., Ajasa, O., Li, T., Waters, M. L., Ginder, G. D., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf439 · Cited by 2
Genome Reorganization during Erythroid Differentiation
Ryzhkova, A. S., & Баттулин, Н. Р. (2021) · Genes · doi:10.3390/genes12071012 · Cited by 2
“In addition to the well-known regulators of erythropoiesis, previously identified via bulk RNAseq in cultured erythroid cells, e.g., KLF1, GATA1, NFE2, BCL11A, LRF, TET2/3, and MYB [49,50], a set of novel regulatory genes have been recognized, that can potentially play a key role in regulating of terminal differentiat…”
Background
Protocols for protein-DNA binding analysis of a zinc finger transcription factor bound to its cognate promoter
Ly, L. C., Yang, Y., Li, F., Crossley, M., Shi, Y., & Quinlan, K. G. R. (2022) · STAR Protocols · doi:10.1016/j.xpro.2022.101598 · Cited by 2
Self-citation
Semiautomated approach focused on new genomic information results in time and effort-efficient reannotation of negative exome data
Ferrer, A., Duffy, P. E., Olson, R. J., Meiners, M. A., Schultz‐Rogers, L. E., Macke, E. L., Safgren, S. L., Morales‐Rosado, J. A., Cousin, M. A., Oliver, G. R., et al. (2024) · Human Genetics · doi:10.1007/s00439-024-02664-3 · Cited by 2
“Furthermore, given the evidence that ZBTB7A transcriptionally represses fetal hemoglobin (HbF), (Masuda 2016) clinical testing of HbF was pursued indicating significantly increased levels in both the proband and the affected brother (8.4 and 4% respectively), consistent with previously described…”
Influential
EryDB: A Transcriptomic Profile Database for Erythropoiesis and Erythroid-related Diseases
Zheng, G., Wu, S., Zhang, Z., Xin, Z., Zhang, L., Zhao, S., Wu, J., Liu, Y., Li, M., Ruan, X., et al. (2024) · Genomics Proteomics & Bioinformatics · doi:10.1093/gpbjnl/qzae029 · Cited by 2
“…in the Disease module, researchers can easily examine the gene expression changes under certain pathological conditions for blood disease diagnosis [38–41], and in the Compounds module, users can obtain information about the small molecules that promote or inhibit erythroid differentiation.”
Post-GWAS Validation of Target Genes Associated with HbF and HbA2 Levels
Caria, C. A., Faà, V., Porcu, S., Marongiu, M. F., Poddie, D., Perseu, L., Meloni, A., Vaccargiu, S., & Ristaldi, M. S. (2024) · Cells · doi:10.3390/cells13141185 · Cited by 2
“…increasing HbF levels has been extensively proven, and key regulators of γ -globin gene (hemoglobin subunit gamma 1/2 [ HBG1/2 [MIM: 142200/142250]) expression, such as BCL11 transcription factor A (BCL11A) or zinc ﬁnger and BTB domain-containing 7A (ZBTB7A/LRF), have been identiﬁed [14–17 , 21].”
Background
Identification of novel BCL11A variant in a patient with developmental delay and behavioural differences
Zha, J., Chen, Y., Cao, F., Zhong, J., Yu, X., & Wu, H. (2024) · International Journal of Developmental Neuroscience · doi:10.1002/jdn.10371 · Cited by 2
“Meanwhile, it has been demonstrated to be a crucial regulator influencing the switch in haemoglobin types and the suppression of HbF (Basak et al., 2015) (Masuda et al., 2016).”
Investigate the Effect of ZFP64 on mRNA Expression of HBG Based on Bioinformatics and Experimental Validation
Huang, S., Wu, J., Yang, Y., Zhu, M., Chen, L., Zhang, S., Yang, Y., Sun, X., & Xie, Y. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01776-5 · Cited by 2
“Therefore, we chose the ZFP64 gene as a research target and performed CRISPR/Cas9 knockout to preliminarily test whether reduced ZFP64 mRNA expression could effectively increase HbF levels [27, 28].”
Single‐Cell Mitochondrial Lineage Tracing Decodes Fate Decision and Spatial Clonal Architecture in Human Hematopoietic Organoids
Xue, Y., Su, J., Chao, Y., Liu, L., Lin, X., Xiang, Y., Ho, M. K., Su, Z., Chen, J., Luo, Z., et al. (2026) · Advanced Science · doi:10.1002/advs.202518084 · Cited by 3
Using microarray analysis to identify genes and pathways that regulate fetal hemoglobin levels
Jia, S., Jia, W., Yu, S., Hu, Y., & He, Y. (2019) · Annals of Human Genetics · doi:10.1111/ahg.12346 · Cited by 2
“HBS1L-MYB, BCL11A, and KLF1 regulate γ-globin gene (HBG1/2) expression and influence HbF levels (Masuda et al., 2016; Sankaran, 2011; Xu et al., 2010).”
Background
Heat shock transcription factor 1 regulates the fetal γ-globin expression in a stress-dependent and independent manner during erythroid differentiation
Gao, J., Liu, J., Zhang, L., Zhang, Y., Guo, Q., Li, Y., Tong, J., Wang, H., Zhou, J., Zhu, F., et al. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.111780 · Cited by 2
The Novel Role of the B-Cell Lymphoma/Leukemia 11A (BCL11A) Gene in β-Thalassaemia Treatment
Lai, M. I., & Ahmed, N. H. M. (2022) · Cardiovascular & Haematological Disorders - Drug Targets · doi:10.2174/1871529x23666230123140926 · Cited by 3

Authors: Masuda, T., Wang, X., Maeda, M., Canver, M. C., Sher, F., Funnell, A. P. W., Fisher, C., Suciu, M., Martyn, G. E., Norton, L. J., Zhu, C., Kurita, R., Nakamura, Y., Xu, J., Higgs, D. R., Crossley, M., Bauer, D. E., Orkin, S. H., Kharchenko, P. V., & Maeda, T.
Affiliations: Brigham and Women's Hospital (US)
Harvard University (US)
Boston Children's Hospital (US)
UNSW Sydney (AU)
Medical Research Council, Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, Oxford University, Oxford, UK.
University of Oxford (GB)
RIKEN BioResource Research Center (JP)
University of Tsukuba (JP)
Corresponding author: Kharchenko, Peter V.
Maeda, Takahiro
ORCID: Masuda, Takeshi
Canver, Matthew C.
Sher, Falak
Funnell, Alister P. W.
Suciu, Maria
Martyn, Gabriella E.
Norton, Laura J.
Zhu, Catherine
Nakamura, Yukio
Xu, Jian
Higgs, Douglas R.
Crossley, Merlin
Bauer, Daniel E.
Orkin, Stuart H.
Kharchenko, Peter V.
Maeda, Takahiro
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2016-01-15
Volume: 351
Issue: 6270
Pages: 285-289
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.aad3312
PMC: PMC4778394
OpenAlex: W2266790363
Semantic Scholar: c79067255bc10df384cd93d45af5c2fd24b7b528
Cited by: 373
References: 64
Citations by year: 2026: 27 · 2025: 34 · 2024: 51 · 2023: 34 · 2022: 34 · 2021: 54 · 2020: 44 · 2019: 24 · 2018: 26 · 2017: 27 · 2016: 16
FWCI: 22.49
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) (F30DK103359-01A1)
NIDDK Career Development (K08DK093705)
Doris Duke Charitable Foundation Innovations in Clinical Research (2013137)
Ellison Medical Foundation (AG-NS-0965-12)
NIH (P01HL032262, P30DK049216, 5K25AG037596, R01 AI084905, R56 DK105001)
American Society of Hematology Bridge Program
Topics: Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: fetal hemoglobin, BCL11A, transcriptional repression, nucleosome density, sickle cell disease, thalassemia, hemoglobinopathies, fetal hemoglobin induction
MeSH terms: Anemia, Sickle Cell, Animals, Carrier Proteins, Cell Line, Chromatin, DNA-Binding Proteins, Erythroblasts, Erythropoiesis, Fetal Hemoglobin, Humans, Nuclear Proteins, Repressor Proteins, Thalassemia, Transcription Factors, Sequence Deletion, Mice, Knockout, Gene Silencing, Mice, gamma-Globins

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Transcription factors LRF and BCL11A independently repress expression of fetal hemoglobin

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