PU.1/Interferon Regulatory Factor Interactions; Mechanisms of Transcriptional Regulation

Marecki, Sylvia; Fenton, Matthew J.

doi:10.1385/cbb:33:2:127

Cited by 74interferon and immune responsesGenomics and Chromatin DynamicsCytokine Signaling Pathways and Interactions

The DOI matches its Crossref record; 117 of the 117 references it cites were found in a registry or an index.

PU.1/Interferon Regulatory Factor Interactions; Mechanisms of Transcriptional Regulation

Marecki, Sylvia, Fenton, Matthew J.·2000·Cell Biochemistry and Biophysics

DOI 10.1385/cbb:33:2:127

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Abstract

The complexity of eukaryotic gene regulation is slowly being resolved. What has become clear is that transcriptional regulation is a multi-step process that involves the assembly of macromolecular complexes. This review will discuss the biology of the ETS family transcription factor PU.1, with emphasis on its interactions with two members of the Interferon Regulatory Factor (IRF) family, interferon consensus sequence binding protein (ICSBP), and IRF-4. The role of these interactions in transcriptional regulation is discussed, with respect to DNA binding motifs, protein-protein interaction and phosphorylation states that modulate PU.1/IRF interactions. Furthermore, potential transcriptional mechanisms for several genes are discussed, focusing on genes involved in innate immunity. Data from these studies suggest at least four distinct paradigms for transcriptional regulation by an ETS protein in conjunction with either ICSBP or IRF-4. These paradigms may describe regulatory mechanisms common to many distinct transcription factor families. Last, recent data from several laboratories have now documented the expression of ICSBP and IRF-4 in a range of cell types. These data suggest that ICSBP and IRF-4 may serve functions within these cell types that are distinct from their previously recognized functions.

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Pip/NF-EM5/IRF-4 is a lymphoid-restricted transcription factor recruited to a composite element (IRF/ETS-binding site) within Ig light chain enhancers through a specific interaction with PU.1 protein.
“Pip/NF-EM5/IRF-4, a member of IRF family, is a lymphoid-restricted transcription factor that is recruited to a composite element (IRF/ETS-binding site) within Ig light chain enhancers through a specific interaction with PU.1 protein [116, 117].”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [116]

HOW CELLS RESPOND TO INTERFERONS
Stark, G. R., Kerr, I. M., Williams, B. R. G., Silverman, R. H., & Schreiber, R. D. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.227 · Cited by 3,932
Requirement of transcription factor PU.1 in the development of multiple hematopoietic lineages
Scott, E. W., Simon, M. C., Anastasi, J., & Singh, H. (1994) · Science · doi:10.1126/science.8079170 · Cited by 1,532
Targeted disruption of the PU.1 gene results in multiple hematopoietic abnormalities
McKercher, S. R., Torbett, B. E., Anderson, K. L., Henkel, G. W., Vestal, D. J., Baribault, H., Klemsz, M., Feeney, A. J., Wu, G. E., Paige, C. J., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00949.x · Cited by 1,130
Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes
Harada, H., Fujita, T., Miyamoto, M., Kimura, Y., Maruyama, M., Furia, A., Miyata, T., & Taniguchi, T. (1989) · Cell · doi:10.1016/0092-8674(89)90107-4 · Cited by 957
Virus-Dependent Phosphorylation of the IRF-3 Transcription Factor Regulates Nuclear Translocation, Transactivation Potential, and Proteasome-Mediated Degradation
Lin, R., Heylbroeck, C., Pitha, P. M., & Hiscott, J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.2986 · Cited by 915
The Ets family of transcription factors
Wasylyk, B., Hahn, S. L., & Giovane, A. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb19864.x · Cited by 839
Regulation of B lymphocyte and macrophage development by graded expression of PU.1
DeKoter, R. P., & Singh, H. (2000) · Science · doi:10.1126/science.288.5470.1439 · Cited by 749
Immunodeficiency and Chronic Myelogenous Leukemia-like Syndrome in Mice with a Targeted Mutation of the ICSBP Gene
Holtschke, T., Löhler, J., Kanno, Y., Fehr, T., Giese, N., Rosenbauer, F., Lou, J., Knobeloch, K.-P., Gabriele, L., Waring, J. F., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81348-3 · Cited by 644
Requirement for the Transcription Factor LSIRF/IRF4 for Mature B and T Lymphocyte Function
Mittrücker, H.-W., Matsuyama, T., Grossman, A., Kündig, T. M., Potter, J., Shahinian, A., Wakeham, A., Patterson, B., Ohashi, P. S., & Mak, T. W. (1997) · Science · doi:10.1126/science.275.5299.540 · Cited by 583
Interferon regulatory factors: the next generation
Mamane, Y., Heylbroeck, C., Génin, P., Algarté-Génin, M., Servant, M. J., Page, C. L., DeLuca, C., Kwon, H., Lin, R., & Hiscott, J. B. (1999) · Gene · doi:10.1016/s0378-1119(99)00262-0 · Cited by 576
Osteopetrosis in mice lacking haematopoietic transcription factor PU.1
Tondravi, M. M., McKercher, S. R., Anderson, K., Erdmann, J. M., Quiroz, M. E., Maki, R. A., & Teitelbaum, S. L. (1997) · Nature · doi:10.1038/386081a0 · Cited by 537
The growing family of interferon regulatory factors
Nguyen, H., Hiscott, J., & Pitha, P. M. (1997) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(97)00019-1 · Cited by 480
Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.
Eisenbeis, C. F., Singh, H., & Storb, U. (1995) · Genes & Development · doi:10.1101/gad.9.11.1377 · Cited by 447
The macrophage transcription factor PU.1 directs tissue-specific expression of the macrophage colony-stimulating factor receptor
Zhang, D.-E., Hetherington, C. J., Chen, H.-M., & Tenen, D. G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.373-381.1994 · Cited by 411
Structure of IRF-1 with bound DNA reveals determinants of interferon regulation
Escalante, C. R., Yie, J., Thanos, D., & Aggarwal, A. K. (1998) · Nature · doi:10.1038/34224 · Cited by 397 · cited 2×
“Several studies suggest that this DBD forms a wHTH structure (68,69).”
Background
Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes.
Au, W.-C., Moore, P. A., Lowther, W. J., Juang, Y., & Pitha, P. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11657 · Cited by 388
An interferon gamma-regulated protein that binds the interferon-inducible enhancer element of major histocompatibility complex class I genes.
Driggers, P. H., Ennist, D. L., Gleason, S. L., Mak, W. H., Marks, M. S., Levi, B. Z., Flanagan, J. R., Appella, E., & Ozato, K. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3743 · Cited by 356
PU.1 recruits a second nuclear factor to a site important for immunoglobulin kappa 3' enhancer activity.
Pongubala, J. M., Nagulapalli, S., Klemsz, M. J., McKercher, S. R., Maki, R. A., & Atchison, M. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.1.368 · Cited by 354
Evidence for a nuclear factor(s), IRF‐1, mediating induction and silencing properties to human IFN‐beta gene regulatory elements.
Fujita, T., Sakakibara, J., Sudo, Y., Miyamoto, M., Kimura, Y., & Taniguchi, T. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03213.x · Cited by 347
Deregulation of MUM1/IRF4 by chromosomal translocation in multiple myeloma
Iida, S., Rao, P. H., Butler, M. P., Corradini, P., Boccadoro, M., Klein, B., CHAGANTI, R. S. K., & Dalla‐Favera, R. (1997) · Nature Genetics · doi:10.1038/ng1097-226 · Cited by 336
A new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex
Kodandapani, R., Pio, F., Ni, C.-Z., Piccialli, G., Klemsz, M., McKercher, S., Maki, R. A., & Ely, K. R. (1996) · Nature · doi:10.1038/380456a0 · Cited by 315
The activation domain of transcription factor PU.1 binds the retinoblastoma (RB) protein and the transcription factor TFIID in vitro: RB shows sequence similarity to TFIID and TFIIB.
Hagemeier, C., Bannister, A. J., Cook, A., & Kouzarides, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1580 · Cited by 303
The proto-oncogene PU.1 regulates expression of the myeloid-specific CD11b promoter
Pahl, H. L., Scheibe, R. J., Zhang, D. E., Chen, H. M., Galson, D. L., Maki, R. A., & Tenen, D. G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53496-7 · Cited by 301
Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation
Pongubala, J., Van Beveren, C., Nagulapalli, S., Klemsz, M., McKercher, Maki, R., & Atchison, M. (1993) · Science · doi:10.1126/science.8456286 · Cited by 271 · cited 15×
“As noted above, PU.1 can also interact with the IRF family members ICSBP and IRF-4 (6,7,17).”
BackgroundInfluential
Regulation of Type I Interferon Gene Expression by Interferon Regulatory Factor-3
Schafer, S. L., Lin, R., Moore, P. A., Hiscott, J. B., & Pitha, P. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.5.2714 · Cited by 266
Sequence and Genomic Analysis of a Rhesus Macaque Rhadinovirus with Similarity to Kaposi’s Sarcoma-Associated Herpesvirus/Human Herpesvirus 8
Searles, R. P., Bergquam, E. P., Axthelm, M. K., & Wong, S. W. (1999) · Journal of Virology · doi:10.1128/jvi.73.4.3040-3053.1999 · Cited by 265
Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
Sirover, M. A. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19970801)66:2 · Cited by 245
Pip, a lymphoid-restricted IRF, contains a regulatory domain that is important for autoinhibition and ternary complex formation with the Ets factor PU.1.
Brass, A. L., Kehrli, E., Eisenbeis, C. F., Storb, U., & Singh, H. (1996) · Genes & Development · doi:10.1101/gad.10.18.2335 · Cited by 242
Regulation of Cell-Type-Specific Interleukin-2 Receptor α-Chain Gene Expression: Potential Role of Physical Interactions between Elf-1, HMG-I(Y), and NF-κ B Family Proteins
John, S., Reeves, R., Lin, J., Child, R., Leiden, J. M., Thompson, C. B., & Leonard, W. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1786 · Cited by 241
Regulation of lymphoid-specific immunoglobulin mu heavy chain gene enhancer by ETS-domain proteins
Nelsen, B., Tian, G., Erman, B., Gregoire, J., Maki, R., Graves, B., & Sen, R. (1993) · Science · doi:10.1126/science.8316859 · Cited by 222
Interferon Consensus Sequence Binding Protein–deficient Mice Display Impaired Resistance to Intracellular Infection Due to a Primary Defect in Interleukin 12 p40 Induction
Scharton-Kersten, T., Contursi, C., Masumi, A., Sher, A., & Ozato, K. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.9.1523 · Cited by 217
Induction of gamma interferon production in human alveolar macrophages by Mycobacterium tuberculosis
Fenton, M. J., Vermeulen, M. W., Kim, S., Burdick, M., Strieter, R. M., & Kornfeld, H. (1997) · Infection and Immunity · doi:10.1128/iai.65.12.5149-5156.1997 · Cited by 209
Self-citation
Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers
Brass, A. L., Zhu, A. Q., & Singh, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.977 · Cited by 204 · cited 1×
“1 and IRF-4 DBDs, connected by a flexible linker, inhibited Ig λ light chain enhancer expression in B cells, implying in vivo binding of this element (110).”
Background
Rel Induces Interferon Regulatory Factor 4 (IRF-4) Expression in Lymphocytes
Grumont, R. J., & Gerondakis, S. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.8.1281 · Cited by 201
Lack of Interferon Consensus Sequence Binding Protein (ICSBP) Transcripts in Human Myeloid Leukemias
Schmidt, M., Nagel, S., Proba, J., Thiede, C., Ritter, M., Waring, J. F., Rosenbauer, F., Huhn, D., Wittig, B., Horak, I., et al. (1998) · Blood · doi:10.1182/blood.v91.1.22 · Cited by 199
Molecular cloning of LSIRF, a lymphoid-specific member of the interferon regulatory factor family that binds the interferon-stimulated response element (ISRE)
Matsuyama, T., Grossman, A., Mittrücker, H.-W., Siderovski, D. P., Kiefer, F., Kawakami, T., Richardson, C. D., Taniguchi, T., Yoshinaga, S. K., & Mak, T. W. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.12.2127 · Cited by 196
A Novel Interferon Regulatory Factor Family Transcription Factor, ICSAT/Pip/LSIRF, That Negatively Regulates the Activity of Interferon-Regulated Genes
Yamagata, T., Nishida, J., Tanaka, T., Sakai, R., Mitani, K., Yoshida, M., Taniguchi, T., Yazaki, Y., & Hirai, H. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1283 · Cited by 196
Myeloid Development Is Selectively Disrupted in PU.1 Null Mice
Anderson, K. L., Smith, K. A., Conners, K., McKercher, S. R., Maki, R. A., & Torbett, B. E. (1998) · Blood · doi:10.1182/blood.v91.10.3702 · Cited by 193
Interferon consensus sequence-binding protein, a member of the interferon regulatory factor family, suppresses interferon-induced gene transcription.
Nelson, N., Marks, M. S., Driggers, P. H., & Ozato, K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.588 · Cited by 192
Interferon Consensus sequence-Binding Protein, a Member of the Interferon Regulatory Factor Family, Suppresses Interferon-Induced Gene Transcription
Nelson, N., Marks, M. S., Driggers, P. H., & Ozato, K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.588-599.1993 · Cited by 192 · cited 2×
“For example, both ICSBP and IRF-4 function as repressors when bound to ISRE elements (53,74).”
Background
Activation of a cell-cycle-regulated histone gene by the oncogenic transcription factor IRF-2
Vaughan, P. S., Aziz, F., van Wijnen, A. J., Wu, S., Harada, H., Taniguchi, T., Soprano, K. J., Stein, J. L., & Stein, G. S. (1995) · Nature · doi:10.1038/377362a0 · Cited by 189
Spi-1/PU.1 Transgenic Mice Develop Multistep Erythroleukemias
Moreau-Gachelin, F., Wendling, F., Molina, T., Denis, N., Titeux, M., Grimber, G., Briand, P., Vainchenker, W., & Tavitian, A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.2453 · Cited by 189
An IFN-γ-Inducible Transcription Factor, IFN Consensus Sequence Binding Protein (ICSBP), Stimulates IL-12 p40 Expression in Macrophages
Wang, I.-M., Contursi, C., Masumi, A., Ma, X., Trinchieri, G., & Ozato, K. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.1.271 · Cited by 187
PU.1 is a component of a multiprotein complex which binds an essential site in the murine immunoglobulin lambda 2-4 enhancer.
Eisenbeis, C. F., Singh, H., & Storb, U. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6452 · Cited by 182
c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription Factor
Behre, G., Whitmarsh, A. J., Coghlan, M. P., Hoang, T., Carpenter, C. L., Zhang, D.-E., Davis, R. J., & Tenen, D. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4939 · Cited by 180
PU.1, Interferon Regulatory Factor 1, and Interferon Consensus Sequence-binding Protein Cooperate to Increase gp91 Expression
Eklund, E. A., Jalava, A., & Kakar, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13957 · Cited by 176
Molecular interactions between interferon consensus sequence binding protein and members of the interferon regulatory factor family.
Bovolenta, C., Driggers, P. H., Marks, M. S., Medin, J. A., Politis, A. D., Vogel, S. N., Levy, D. E., Sakaguchi, K., Appella, E., & Coligan, J. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.5046 · Cited by 167
Interferon Regulatory Factor-2 Is a Transcriptional Activator in Muscle Where It Regulates Expression of Vascular Cell Adhesion Molecule-1
Jesse, T. L., LaChance, R., Iademarco, M. F., & Dean, D. C. (1998) · Journal of Cell Biology · doi:10.1083/jcb.140.5.1265 · Cited by 167
Induction of IFN-γ in macrophages by lipopolysaccharide
Fultz, M. J., Barber, S. A., Dieffenbach, C. W., & Vogel, S. N. (1993) · International Immunology · doi:10.1093/intimm/5.11.1383 · Cited by 165
Phosphorylation Events Modulate the Ability of Interferon Consensus Sequence Binding Protein to Interact with Interferon Regulatory Factors and to Bind DNA
Sharf, R., Meraro, D., Azriel, A., Thornton, A. M., Ozato, K., Petricoin, E. F., Larner, A. C., Schaper, F., Hauser, H., & Levi, B.-Z. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9785 · Cited by 162
Interferon (IFN) Consensus Sequence-binding Protein, a Transcription Factor of the IFN Regulatory Factor Family, Regulates Immune Responses In Vivo through Control of Interleukin 12 Expression
Giese, N. A., Gabriele, L., Doherty, T. M., Klinman, D. M., Tadesse-Heath, L., Contursi, C., Epstein, S. L., & Morse, H. C. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.9.1535 · Cited by 160
Role of PU.1 in Hematopoiesis
Fisher, R. C., & Scott, E. W. (1998) · STEM CELLS · doi:10.1002/stem.160025 · Cited by 158
Human interferon consensus sequence binding protein is a negative regulator of enhancer elements common to interferon-inducible genes.
Weisz, A., Marx, P., Sharf, R., Appella, E., Driggers, P. H., Ozato, K., & Levi, B. Z. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74081-2 · Cited by 152
The transcription factor PU.1 is involved in macrophage proliferation.
Celada, A., Borràs, F. E., Soler, C., Lloberas, J., Klemsz, M., van Beveren, C., McKercher, S., & Maki, R. A. (1996) · The Journal of experimental medicine · doi:10.1084/jem.184.1.61 · Cited by 152 · cited 4×
“In some instances, binding of both factors to DNA is required; in others, PU.1 may actually tether another factor to the DNA, as has been reported for c-Jun on the M-CSF promoter and C/EBPβ on the IL-1β promoter (35,36).”
BackgroundInfluential
Differential regulation of interstitial collagenase (MMP-1) gene expression by ETS transcription factors
Westermarck, J. K., Seth, A. K., & Kähäri, V. (1997) · Oncogene · doi:10.1038/sj.onc.1201111 · Cited by 149
Protein-Protein and DNA-Protein Interactions Affect the Activity of Lymphoid-Specific IFN Regulatory Factors
Meraro, D., Hashmueli, S., Koren, B., Azriel, A., Oumard, A., Kirchhoff, S., Hauser, H., Nagulapalli, S., Atchison, M. L., & Levi, B.-Z. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.12.6468 · Cited by 147
Monocyte Expression of the Human Prointerleukin 1β Gene (IL1B) Is Dependent on Promoter Sequences Which Bind the Hematopoietic Transcription Factor Spi-1/PU.1
Kominato, Y., Galson, D. L., Waterman, W. R., Webb, A. C., & Auron, P. E. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.59 · Cited by 146
ETS1, NFκB and AP1 synergistically transactivate the human GM – CSF promoter
Thomas, R. S., Tymms, M. J., McKinlay, L. H., Shannon, M. F., Seth, A. K., & Kola, I. (1997) · Oncogene · doi:10.1038/sj.onc.1201125 · Cited by 145
Expression of Interferon Consensus Sequence Binding Protein (ICSBP) Is Downregulated in Bcr-Abl-Induced Murine Chronic Myelogenous Leukemia-Like Disease, and Forced Coexpression of ICSBP Inhibits Bcr-Abl-Induced Myeloproliferative Disorder
Hao, S. X., & Ren, R. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1149-1161.2000 · Cited by 143
Physical interactions between Ets and NF-kappaB/NFAT proteins play an important role in their cooperative activation of the human immunodeficiency virus enhancer in T cells
Bassuk, A. G., Anandappa, R. T., & Leiden, J. M. (1997) · Journal of Virology · doi:10.1128/jvi.71.5.3563-3573.1997 · Cited by 136
Transactivation of Classical and Nonclassical HLA Class I Genes Through the IFN-Stimulated Response Element
Gobin, S. J. P., van Zutphen, M., Woltman, A. M., & van den Elsen, P. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.3.1428 · Cited by 136
Protein tyrosine kinase Pyk2 mediates the Jak‐dependent activation of MAPK and Stat1 in IFN‐γ, but not IFN‐α, signaling
Takaoka, A., Tanaka, N., Mitani, Y., Miyazaki, T., Fujii, H., Sato, M., Kovarik, P., Decker, T., Schlessinger, J., & Taniguchi, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.9.2480 · Cited by 133
Unique properties of a second human herpesvirus 8-encoded interferon regulatory factor (vIRF-2).
Burýšek, L., Yeow, W.-S., & Pitha, P. M. (1999) · PubMed · Cited by 127
The Histone Acetylase PCAF Is a Phorbol-Ester-Inducible Coactivator of the IRF Family That Confers Enhanced Interferon Responsiveness
Masumi, A., Wang, I.-M., Lefebvre, B., Yang, X.-J., Nakatani, Y., & Ozato, K. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1810 · Cited by 124
Interferon regulatory factor subcellular localization is determined by a bipartite nuclear localization signal in the DNA-binding domain and interaction with cytoplasmic retention factors.
Lau, J. F., Parisien, J.-P., & Horvath, C. M. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.97.13.7278 · Cited by 120
IL-12 Is Dysregulated in Macrophages from IRF-1 and IRF-2 Knockout Mice
Salkowski, C. A., Kopydlowski, K., Blanco, J., Cody, M. J., McNally, R., & Vogel, S. N. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.3.1529 · Cited by 119
The Ets protein Spi-B is expressed exclusively in B cells and T cells during development.
Su, G. H., Ip, H. S., Cobb, B. S., Lu, M. M., Chen, H. M., & Simon, M. C. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.1.203 · Cited by 113
Physical and functional interactions between the transcription factor PU.1 and the coactivator CBP
Yamamoto, H., Kihara-Negishi, F., Yamada, T., Hashimoto, Y., & Oikawa, T. (1999) · Oncogene · doi:10.1038/sj.onc.1202427 · Cited by 113 · cited 3×
“1 has been reported to interact with the histone acetylase CREB binding protein (CBP) (16), implicating PU.”
BackgroundInfluential
Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 β (C/EBP δ, CRP3)
Nagulapalli, S., Pongubala, J. M., & Atchison, M. L. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.155.9.4330 · Cited by 110
Spi-1/PU.1: an oncogene of the Ets family
Moreau-Gachelin, F. (1994) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(94)90011-6 · Cited by 110
Stimulation of macrophages by lipopolysaccharide alters the phosphorylation state, conformation, and function of PU.1 via activation of casein kinase II
Lodie, T. A., Savedra, R., Golenbock, D. T., Van Beveren, C. P., Maki, R. A., & Fenton, M. J. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.4.1848 · Cited by 106
Self-citation
Roles of IFN Consensus Sequence Binding Protein and PU.1 in Regulating IL-18 Gene Expression
Kim, Y.-M., Kang, H.-S., Paik, S., Pyun, K.-H., Anderson, K. L., Torbett, B. E., & Choi, I. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.4.2000 · Cited by 103
Functional Domain Analysis of Interferon Consensus Sequence Binding Protein (ICSBP) and Its Association with Interferon Regulatory Factors
Sharf, R., Azriel, A., Lejbkowicz, F., Winograd, S. S., Ehrlich, R., & Levi, B.-Z. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13063 · Cited by 100
PU.1 as an essential activator for the expression of gp91 phox gene in human peripheral neutrophils, monocytes, and B lymphocytes
Suzuki, S., Kumatori, A., Haagen, I.-A., Fujii, Y., Sadat, M., Jun, H. L., Tsuji, Y., Roos, D., & Nakamura, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6085 · Cited by 99
DNA Binding Specificity Studies of Four ETS Proteins Support an Indirect Read-out Mechanism of Protein-DNA Recognition
Szymczyna, B. R., & Arrowsmith, C. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004294200 · Cited by 99
NF-IL6 (C/EBPβ) Vigorously Activates il1b Gene Expression via a Spi-1 (PU.1) Protein-Protein Tether
Yang, Z., Wara-aswapati, N., Chen, C., Tsukada, J., & Auron, P. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000145200 · Cited by 92
Differential Expression and Distinct Functions of IFN Regulatory Factor 4 and IFN Consensus Sequence Binding Protein in Macrophages
Marecki, S., Atchison, M. L., & Fenton, M. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2713 · Cited by 87
Self-citation
PU.1 can participate in an active enhancer complex without its transcriptional activation domain
Pongubala, J. M. R., & Atchison, M. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.1.127 · Cited by 86
Cell-specific expression of the macrophage scavenger receptor gene is dependent on PU.1 and a composite AP-1/ets motif.
Moulton, K. S., Semple, K., Wu, H., & Glass, C. K. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4408 · Cited by 86
Molecular cloning of a novel interferon regulatory factor in Japanese flounder, Paralichthys olivaceus.
Yabu, T., Hirose, H., Hırono, I., Katagiri, T., Aoki, T., & Yamamoto, E. (1998) · PubMed · Cited by 83
New Insights on DNA Recognition by ets Proteins from the Crystal Structure of the PU.1 ETS Domain-DNA Complex
Pio, F., Kodandapani, R., Ni, C.-Z., Shepard, W., Klemsz, M., McKercher, S. R., Maki, R. A., & Ely, K. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23329 · Cited by 81
A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity
Lin, R., Lin, R., Hiscott, J. B., Hiscott, J. B., & Hiscott, J. B. (1999) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006850009017 · Cited by 77
A Two-Step Mechanism for Recruitment of Pip by PU.1
Perkel, J. M., & Atchison, M. L. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.1.241 · Cited by 77
A Novel STAT-Like Factor Mediates Lipopolysaccharide, Interleukin 1 (IL-1), and IL-6 Signaling and Recognizes a Gamma Interferon Activation Site-Like Element in the IL1B Gene
Tsukada, J., Waterman, W. R., Koyama, Y., Webb, A. C., & Auron, P. E. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.2183 · Cited by 77
IFN consensus sequence binding protein potentiates STAT1-dependent activation of IFNγ-responsive promoters in macrophages
Contursi, C., Wang, I.-M., Gabriele, L., Gadina, M., O'Shea, J., Morse, H. C., & Ozato, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.91 · Cited by 72
Modulation of interferon consensus sequence binding protein mRNA in murine peritoneal macrophages. Induction by IFN-gamma and down-regulation by IFN-alpha, dexamethasone, and protein kinase inhibitors
Politis, A. D., Sivo, J., Driggers, P. H., Ozato, K., & Vogel, S. N. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.148.3.801 · Cited by 68 · cited 1×
“IRF-4 expression does not appear to be modulated by IFN-γ stimulation, whereas ICSBP expression is strongly induced (53,77).”
Background
PU.1/Pip and Basic Helix Loop Helix Zipper Transcription Factors Interact With Binding Sites in the CD20 Promoter to Help Confer Lineage- and Stage-Specific Expression of CD20 in B Lymphocytes
Himmelmann, A., Riva, A., Wilson, G. L., Lucas, B. P., Thevenin, C., & Kehrl, J. H. (1997) · Blood · doi:10.1182/blood.v90.10.3984 · Cited by 68
Interferon Regulatory Factor-2 Directs Transcription from the gp91 Promoter
Luo, W., & Skalnik, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23445 · Cited by 67
Regulation of IFN Consensus Sequence Binding Protein Expression in Murine Macrophages
Kantakamalakul, W., Politis, A. D., Marecki, S., Sullivan, T., Ozato, K., Fenton, M. J., & Vogel, S. N. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.12.7417 · Cited by 61
Self-citation
Regulation of IFN-gamma-induced nuclear expression of IFN consensus sequence binding protein in murine peritoneal macrophages.
Politis, A. D., Ozato, K., Coligan, J. E., & Vogel, S. N. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.5.2270 · Cited by 61
Cloning of Human Lymphocyte-Specific Interferon Regulatory Factor (hLSIRF/hIRF4) and Mapping of the Gene to 6p23–p25
Grossman, A., Mittrücker, H.-W., Nicholl, J., Suzuki, A., Chung, S., Antonio, L., Suggs, S., Sutherland, G. R., Siderovski, D. P., & Mak, T. W. (1996) · Genomics · doi:10.1006/geno.1996.0547 · Cited by 60
The [(G/C)3NN]n motif: a common DNA repeat that excludes nucleosomes.
Wang, Y. H., & Griffith, J. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.17.8863 · Cited by 56
Commitment to the Monocytic Lineage Occurs in the Absence of the Transcription Factor PU.1
Henkel, G. W., McKercher, S. R., Leenen, P. J. M., & Maki, R. A. (1999) · Blood · doi:10.1182/blood.v93.9.2849 · Cited by 53
Spi-C, a Novel Ets Protein That Is Temporally Regulated during B Lymphocyte Development
Bemark, M., Mårtensson, A., Liberg, D., & Leanderson, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.10259 · Cited by 52
ETS Protein–Dependent Accessibility Changes at the Immunoglobulin μ Heavy Chain Enhancer
Nikolajczyk, B. S., Sanchez, J. A., & Sen, R. (1999) · Immunity · doi:10.1016/s1074-7613(00)80077-1 · Cited by 51
IFN consenus sequence binding protein (ICSBP) is a conditional repressor of IFN inducible promoters
Welsz, A., Kirchhoff, S., & Levi, B.-Z. (1994) · International Immunology · doi:10.1093/intimm/6.8.1125 · Cited by 50 · cited 1×
“Some of these genes include MHC-I (H-2Ld), 2′-5′-oligo-adenylate synthetase (OAS) and interferon-stimulated gene 54 (ISG54) (74,79,80).”
Background
Normal Myeloid Development Requires Both the Glutamine-Rich Transactivation Domain and the PEST Region of Transcription Factor PU.1 but Not the Potent Acidic Transactivation Domain
Fisher, R. C., Olson, M. C., Pongubala, J. M. R., Perkel, J. M., Atchison, M. L., Scott, E. W., & Simon, M. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.4347 · Cited by 49
SPI-B Activates Transcription via a Unique Proline, Serine, and Threonine Domain and Exhibits DNA Binding Affinity Differences from PU.1
Rao, S., Matsumura, A., Yoon, J. W., & Simon, M. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.11115 · Cited by 46
Mutation analysis of the Pip interaction domain reveals critical residues for protein–protein interactions
Ortiz, M. A., Light, J. P., Maki, R. A., & Assa‐Munt, N. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2740 · Cited by 44
DNA Methylation and Chromatin Structure Regulate PU.1 Expression
Amaravadi, L., & Klemsz, M. J. (1999) · DNA and Cell Biology · doi:10.1089/104454999314737 · Cited by 44
IP-10 Gene Transcription by Virus in Astrocytes Requires Cooperation of ISRE with Adjacent κB Site but Not IRF-1 or Viral Transcription
Cheng, G., NAZAR, A. S. M. I., Shin, H. S., Vanguri, P., & Shin, M. L. (1998) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1998.18.987 · Cited by 43
Repression of I-Aβ Gene Expression by the Transcription Factor PU.1
Borràs, F. E., Lloberas, J., Maki, R. A., & Celada, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24385 · Cited by 40
Both PU.1 and nuclear factor-kappa B mediate lipopolysaccharide- induced HIV-1 long terminal repeat transcription in macrophages.
Lodie, T. A., Reiner, M., Coniglio, S. J., Viglianti, G. A., & Fenton, M. J. (1998) · PubMed · Cited by 39
Self-citation
The NF-beta A-binding element, not an overlapping NF-IL-6-binding element, is required for maximal IL-1 beta gene expression.
Buras, J. A., Monks, B. G., & Fenton, M. J. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.9.4444 · Cited by 39
Self-citation
Cooperative interaction between the DNA-binding domains of PU.1 and IRF4
Yee, A. A., Yin, P., Siderovski, D. P., Mak, T. W., Litchfield, D. W., & Arrowsmith, C. H. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1838 · Cited by 38
PU.1 negatively regulates the CD11c integrin gene promoter through recognition of the major transcriptional start site
López‐Rodríguez, C., & Corbí, A. L. (1997) · European Journal of Immunology · doi:10.1002/eji.1830270804 · Cited by 36
Role of Asymmetric Phosphate Neutralization in DNA Bending by PU.1
Strauss-Soukup, J. K., & Maher, L. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31570 · Cited by 31
PU.1 and USF Are Required for Macrophage-specific Mannose Receptor Promoter Activity
Egan, B. S., Lane, K. B., & Shepherd, V. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.9098 · Cited by 30
Interferon Consensus Sequence-binding Protein Is Constitutively Expressed and Differentially Regulated in the Ocular Lens
Li, W., Nagineni, C. N., Ge, H., Efiok, B. J. S., Chepelinsky, A. B., & Egwuagu, C. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9686 · Cited by 28
Interferon-gamma signaling in human retinal pigment epithelial cells mediated by STAT1, ICSBP, and IRF-1 transcription factors.
Li, W., Nagineni, C. N., Hooks, J. J., Chepelinsky, A. B., & Egwuagu, C. E. (1999) · PubMed · Cited by 25
Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix–turn–helix family
Furui, J., Uegaki, K., Yamazaki, T., Shirakawa, M., Swindells, M. B., Harada, H., Taniguchi, T., & Kyogoku, Y. (1998) · Structure · doi:10.1016/s0969-2126(98)00050-1 · Cited by 25
Transcription Factor PU.1 Mediates Induction of c- fms in Vascular Smooth Muscle Cells: a Mechanism for Phenotypic Change to Phagocytic Cells
Inaba, T., Gotoda, T., Ishibashi, S., Harada, K., Ohsuga, J.-I., Ohashi, K., Yazaki, Y., & Yamada, N. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.2264 · Cited by 24
Identification of the secretory leukocyte protease inhibitor (SLPI) as a target of IRF-1 regulation
Nguyen, H., Teskey, L., Lin, R., & Hiscott, J. B. (1999) · Oncogene · doi:10.1038/sj.onc.1202924 · Cited by 24
NFβA, a factor required for maximal interleukin-1β gene expression is identical to the ets family member PU.1. Evidence for structural alteration following LPS activation
Buras, J. A., Reenstra, W. R., & Fenton, M. J. (1995) · Molecular Immunology · doi:10.1016/0161-5890(95)00018-a · Cited by 23
Self-citation
Quantitative Hydroxyl Radical Footprinting Reveals Cooperative Interactions between DNA-Binding Subdomains of PU.1 and IRF4
Gross, P., Yee, A. A., Arrowsmith, C. H., & Macgregor, R. B. (1998) · Biochemistry · doi:10.1021/bi9731448 · Cited by 23
Signaling Pathways Mediated by the TNF- and Cytokine-Receptor Families Target a Common cis-Element of the IFN Regulatory Factor 1 Promoter
Gupta, S. K., Xia, D., Jiang, M., Lee, S.-J., & Pernis, A. B. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.11.5997 · Cited by 23
In vivo formation of IRF-1 homodimers
Kirchhoff, S., Schaper, F., Oumard, A., & Häuser, H. (1998) · Biochimie · doi:10.1016/s0300-9084(99)80019-4 · Cited by 20

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Exploiting Synthetic Lethality for the Therapy of ABC Diffuse Large B Cell Lymphoma
Yang, Y., Shaffer, A. L., Emre, N. C. T., Ceribelli, M., Zhang, M., Wright, G. W., Xiao, W., Powell, J. I., Platig, J., Kohlhammer, H., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.024 · Cited by 540
Interferon regulatory factor-8 regulates bone metabolism by suppressing osteoclastogenesis
Zhao, B., Takami, M., Yamada, A., Wang, X., Koga, T., Hu, X., Tamura, T., Ozato, K., Choi, Y., Ivashkiv, L. B., et al. (2009) · Nature Medicine · doi:10.1038/nm.2007 · Cited by 316
The impact of interferon-regulatory factors to macrophage differentiation and polarization into M1 and M2
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PU.1 regulates the commitment of adult hematopoietic progenitors and restricts granulopoiesis
Dakic, A., Metcalf, D., Di Rago, L., Mifsud, S., Wu, L., & Nutt, S. L. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050075 · Cited by 297
Toll-Like Receptor Signaling and Regulation of Cytokine Gene Expression in the Immune System
Ozato, K., Tsujimura, H., & Tamura, T. (2002) · BioTechniques · doi:10.2144/oct0208 · Cited by 189
Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells
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Direct Inhibition of IRF-Dependent Transcriptional Regulatory Mechanisms Associated With Disease
Antonczyk, A., Krist, B., Sajek, M., Sekrecka, A., Piaszyk-Borychowska, A., Plens-Gałąska, M., Wesoły, J., & Bluyssen, H. A. R. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01176 · Cited by 162
Dynamic Evolution of Immune System Regulators: The History of the Interferon Regulatory Factor Family
Nehyba, J., Hrdličková, R., & Bose, H. R. (2009) · Molecular Biology and Evolution · doi:10.1093/molbev/msp167 · Cited by 153
When Ets transcription factors meet their partners
Verger, A., & Duterque‐Coquillaud, M. (2002) · BioEssays · doi:10.1002/bies.10068 · Cited by 134
Monocyte differentiation and macrophage polarization
Orekhov, A. N., Orekhova, V. A., Nikiforov, N. G., Myasoedova, V. A., Grechko, A. V., Romanenko, E. B., Zhang, D., & Chistiakov, D. A. (2019) · Vessel Plus · doi:10.20517/2574-1209.2019.04 · Cited by 144
B Lymphocyte-Induced Maturation Protein (Blimp)-1, IFN Regulatory Factor (IRF)-1, and IRF-2 Can Bind to the Same Regulatory Sites
Kuo, T. C., & Calame, K. L. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5556 · Cited by 132
Immune cell-specific amplification of interferon signaling by the IRF-4/8-PU. 1 complex
Kanno, Y., Levi, B.-Z., Tamura, T., & Ozato, K. (2005) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2005.25.770 · Cited by 128
Virus-induced Heterodimer Formation betweenIRF-5 and IRF-7 Modulates Assembly of theIFNA Enhanceosome in Vivo and Transcriptional Activity of IFNA Genes
Barnes, B. J., Field, A. E., & Pitha-Rowe, P. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212609200 · Cited by 119
Transcription factor PU.1 represses and activates gene expression in early T cells by redirecting partner transcription factor binding
Hosokawa, H., Ungerbäck, J., Wang, X., Matsumoto, M., Nakayama, K. I., Cohen, S. M., Tanaka, T., & Rothenberg, E. V. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.024 · Cited by 116
Differential Expression of IFN Regulatory Factor 4 Gene in Human Monocyte-Derived Dendritic Cells and Macrophages
Lehtonen, A., Veckman, V., Nikula, T., Lahesmaa, R., Kinnunen, L., Matikainen, S., & Julkunen, I. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.10.6570 · Cited by 120
PU.1 and Multiple IFN Regulatory Factor Proteins Synergize to Mediate Transcriptional Activation of the Human IL-1β Gene
Marecki, S., Riendeau, C. J., Liang, M. D., & Fenton, M. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.11.6829 · Cited by 111
Self-citation
IFN-Stimulated Gene 15 Is Synergistically Activated Through Interactions Between the Myelocyte/Lymphocyte-Specific Transcription Factors, PU.1, IFN Regulatory Factor-8/IFN Consensus Sequence Binding Protein, and IFN Regulatory Factor-4: Characterization of a New Subtype of IFN-Stimulated Response Element
Meraro, D., Gleit-Kielmanowicz, M., Hauser, H., & Levi, B.-Z. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.12.6224 · Cited by 105
Mechanisms of Action of Hematopoietic Transcription Factor PU.1 in Initiation of T-Cell Development
Rothenberg, E. V., Hosokawa, H., & Ungerbäck, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00228 · Cited by 99
Transcription factor PU.1 and immune cell differentiation (Review)
Li, G., Hao, W., & Hu, W. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4763 · Cited by 98
Regulation of human β2-microglobulin transactivation in hematopoietic cells
Gobin, S. J. P., Biesta, P. J., & van den Elsen, P. J. (2003) · Blood · doi:10.1182/blood-2002-09-2924 · Cited by 86
TREM‐1 expression in macrophages is regulated at transcriptional level by NF‐κB and PU.1
Zeng, H., Ornatowska, M., Joo, M., & Sadikot, R. T. (2007) · European Journal of Immunology · doi:10.1002/eji.200737270 · Cited by 88
Identification of IRF-8 and IRF-1 target genes in activated macrophages
Dror, N., Alter-Koltunoff, M., Azriel, A., Amariglio, N., Jacob‐Hirsch, J., Zeligson, S., Morgenstern, A., Tamura, T., Häuser, H., Rechavi, G., et al. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.02.026 · Cited by 79
PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis
Gupta, P., Gurudutta, G. U., Saluja, D., & Tripathi, R. P. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00757.x · Cited by 74
Is PU.1 a dosage-sensitive regulator of haemopoietic lineage commitment and leukaemogenesis?
Dakic, A., Wu, L., & Nutt, S. L. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.01.006 · Cited by 72
Review: ICSBP/IRF-8 Transactivation: A Tale of Protein-Protein Interaction
Levi, B.-Z., Hashmueli, S., Gleit-Kielmanowicz, M., Azriel, A., & Meraro, D. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452764 · Cited by 70
Molecular Mechanisms for Synchronized Transcription of Three Complement C1q Subunit Genes in Dendritic Cells and Macrophages*
Chen, G.-B., Tan, C., Teh, B. K., & Lu, J.-H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.286427 · Cited by 70
Positive Regulatory Domain I (PRDM1) and IRF8/PU.1 Counter-regulate MHC Class II Transactivator (CIITA) Expression during Dendritic Cell Maturation
Smith, M. A., Wright, G. M., Wu, J., Tailor, P. B., Ozato, K., Chen, X., Wei, S., Piskurich, J. F., Ting, J. P. ‐., & Wright, K. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.165431 · Cited by 63
Regulation of IFN Regulatory Factor 4 Expression in Human T Cell Leukemia Virus-I-Transformed T Cells
Sharma, S., Grandvaux, N., Mamane, Y., Génin, P., Azimi, N., Waldmann, T. A., & Hiscott, J. B. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.6.3120 · Cited by 61
E47, IRF-4, and PU.1 synergize to induce B-cell-specific activation of the class II transactivator promoter III (CIITA-PIII)
van der Stoep, N., Quinten, E., Rezende, M. M., & van den Elsen, P. J. (2004) · Blood · doi:10.1182/blood-2004-03-0790 · Cited by 58
IRF8 Governs Expression of Genes Involved in Innate and Adaptive Immunity in Human and Mouse Germinal Center B Cells
Shin, D., Lee, C., & Morse, H. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027384 · Cited by 59
The interferon regulatory factor ICSBP/IRF-8 in combination with PU.1 up-regulates expression of tumor suppressor p15Ink4b in murine myeloid cells
Schmidt, M., Bies, J., Tamura, T., Ozato, K., & Wolff, L. (2004) · Blood · doi:10.1182/blood-2003-01-0285 · Cited by 58
PU.1 and ICSBP control constitutive and IFN-γ-regulatedTlr9gene expression in mouse macrophages
Schroder, K., Lichtinger, M., Irvine, K. M., Brion, K., Trieu, A., Ross, I. L., Ravasi, T., Stacey, K. J., Rehli, M., Hume, D. A., et al. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0107036 · Cited by 51
Double‐stranded RNA activates RANTES gene transcription through co‐operation of nuclear factor‐κB and interferon regulatory factors in human airway epithelial cells
Ieki, K., Matsukura, S., Kokubu, F., Kimura, T., Kuga, H., Kawaguchi, M., Odaka, M., Suzuki, S., Watanabe, S., Takeuchi, H. T., et al. (2004) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2004.1941.x · Cited by 48
Partner-regulated interaction of IFN regulatory factor 8 with chromatin visualized in live macrophages
Laricchia‐Robbio, L., Tamura, T., Karpova, T., Sprague, B. L., McNally, J. G., & Ozato, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504014102 · Cited by 48
Transcriptional Regulation of Mouse μ Opioid Receptor Gene by PU.1
Hwang, C. K., Kim, C. S., Choi, H. S., McKercher, S. R., & Loh, H. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400755200 · Cited by 46
Activation of the innate immune response and interferon signalling in myotonic dystrophy type 1 and type 2 cataracts
Rhodes, J. D., Lott, M. C., Russell, S., Moulton, V., Sanderson, J., Wormstone, I. M., & Broadway, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr515 · Cited by 47
Origins of lymphocyte developmental programs: transcription factor evidence
Rothenberg, E. V., & Pant, R. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.08.002 · Cited by 42
Nramp1-mediated Innate Resistance to Intraphagosomal Pathogens Is Regulated by IRF-8, PU.1, and Miz-1
Alter-Koltunoff, M., Ehrlich, S., Dror, N., Azriel, A., Eilers, M., Häuser, H., Bowen, H., Barton, C. H., Tamura, T., Ozato, K., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307954200 · Cited by 42
Specificity and Function of IRF Family Transcription Factors: Insights from Genomics
Mancino, A., & Natoli, G. (2016) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2016.0004 · Cited by 39
ERK Activation Is Required for Double-stranded RNA- and Virus-induced Interleukin-1 Expression by Macrophages
Maggi, L. B., Moran, J. M., Buller, R. M. L., & Corbett, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211744200 · Cited by 40
The transcription factor Spi-B regulates human plasmacytoid dendritic cell survival through direct induction of the antiapoptotic gene BCL2-A1
Karrich, J. J., Balzarolo, M., Schmidlin, H., Libouban, M. A. A., Nagasawa, M., Gentek, R., Kamihira, S., Maeda, T., Amsen, D., Wolkers, M. C., et al. (2012) · Blood · doi:10.1182/blood-2011-07-370239 · Cited by 42
Repression of IRF-4 target genes in human T cell leukemia virus-1 infection
Mamane, Y., Grandvaux, N., Hernandez, E., Sharma, S., Innocente, S. A., Lee, J. M., Azimi, N., Lin, R., & Hiscott, J. B. (2002) · Oncogene · doi:10.1038/sj.onc.1205843 · Cited by 35
Identification and characterization of a PU.1/Spi-B binding site in the bovine leukemia virus long terminal repeat
Dekoninck, A., Calomme, C., Nizet, S., de Launoit, Y., Burny, A., Ghysdael, J., & Lint, C. M. V. (2003) · Oncogene · doi:10.1038/sj.onc.1206392 · Cited by 35
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Yashiro, T., Yamamoto, M., Araumi, S., Hara, M., Yogo, K., Uchida, K., Kasakura, K., & Nishiyama, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.649572 · Cited by 31
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Yoon, H., & Boss, J. M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000079 · Cited by 29
Review: IRF-4 Activities in HTLV-I-Induced T Cell Leukemogenesis
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Xia, X., Wang, W., Yin, K., & Wang, S. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.03.003 · Cited by 23
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Marden, C. M., Stefanidis, D., Cunninghame‐Graham, D. S., & Casimir, C. M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00727-7 · Cited by 13
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Vitezic, M. (2013) · Figshare
Transcription Factors: Deciphering the Transcription Factor Network of Dendritic Cell Development
Hieronymus, T., & Zenke, M. (2006) · Wiley eBooks · doi:10.1002/9783527619696.ch4
Expression and activation of STAT and IRF family transcription factors in mononuclear leukocytes
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Roles for Pin1 in Modulating Cells of the Innate Immune System
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The Transcriptional Regulation of HLA-E by Interferon-Gamma in Tumor Cells
Grant, Q. (2010) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/9hab-qt04

Mechanisms of Transcriptional Regulation
Marecki, S., & Fenton, M. J. (2000) · Cited by 2
Self-citation
Analysis of PU.1/ICSBP (IRF-8) complex formation with various PU.1 mutants: molecular cloning of rat Icsbp (Irf-8) cDNA
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Meraro, D., Hashmueli, S., Koren, B., Azriel, A., Oumard, A., Kirchhoff, S., Hauser, H., Nagulapalli, S., Atchison, M. L., & Levi, B.-Z. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.12.6468 · Cited by 147
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Self-citation

Authors: Marecki, S., & Fenton, M. J.
Affiliations: Boston University (US)
ORCID: Fenton, Matthew J.
Venue: Cell Biochemistry and Biophysics
Publisher: Springer Science and Business Media LLC
Published: 2000
Volume: 33
Issue: 2
Pages: 127-148
ISSN: 1085-9195 (ISSN-L)
DOI: 10.1385/cbb:33:2:127
OpenAlex: W2330690422
Semantic Scholar: 1f32d4a50efbfa831a0783908370cea0e52d57cd
Cited by: 74
References: 117
Citations by year: 2025: 1 · 2024: 1 · 2022: 4 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 1 · 2016: 1 · 2015: 1 · 2013: 1 · 2012: 3
FWCI: 2.00
Type: journal article
Language: en
Open access: closed
Locations: Cell Biochemistry and Biophysics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Keywords: PU.1, interferon regulatory factors, IRF8, IRF4, ETS transcription factors, transcriptional regulation, protein-protein interaction, phosphorylation, DNA-binding motifs, innate immunity, transcription factor complex
MeSH terms: Interferon Regulatory Factor-8, Interferon Regulatory Factor-4, Proto-Oncogene Protein Spi-1, Animals, Binding Sites, DNA, DNA-Binding Proteins, Gene Expression Regulation, Humans, Interferons, Proto-Oncogene Proteins, Repetitive Sequences, Nucleic Acid, Repressor Proteins, Transcription Factors, Transcription, Genetic, Trans-Activators, Consensus Sequence, Proto-Oncogene Proteins c-ets, Interferon Regulatory Factors

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PU.1/Interferon Regulatory Factor Interactions; Mechanisms of Transcriptional Regulation

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