Physical and functional interactions between the transcription factor PU.1 and the coactivator CBP

Yamamoto, Hitomi; Kihara-Negishi, Fumiko; Yamada, Toshiyuki; Hashimoto, Yoshiyuki; Oikawa, Tsuneyuki

doi:10.1038/sj.onc.1202427

Cited by 111Genomics and Chromatin DynamicsHematopoietic Stem Cell TransplantationCytokine Signaling Pathways and Interactions

Physical and functional interactions between the transcription factor PU.1 and the coactivator CBP

Yamamoto, Hitomi, Kihara-Negishi, Fumiko, Yamada, Toshiyuki, Hashimoto, Yoshiyuki, Oikawa, Tsuneyuki·1999·Oncogene

DOI 10.1038/sj.onc.1202427

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Abstract

Yeast two-hybrid system was employed to isolate novel proteins that physically interact with PU.1, a member of Ets family transcription factors. Sequence analyses of several isolated clones positive for beta-galactosidase activity revealed that one of these clones was confirmed to encode a transcriptional coactivator, CREB binding protein (CBP). GST binding assay showed that the interacting sites were located at the transcriptional activation domain of PU.1 through 74-122 and the region spanning residues 1283-1915 of CBP. CBP potentiated PU.1-mediated transcription of the reporter gene driven by the multimerized PU.1-binding sites, suggesting that CBP functions as a coactivator for PU.1. Considering that CBP is a limited cellular component to function as a coactivator for several transcription factors, CBP may mediate synergistic and antagonistic interactions between PU.1 and other transcription factors during the process of hematopoietic cell differentiation.

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PU.1 can interact with CBP/p300 and TRIM33.
“as PU.1 can interact with CBP/p300 (refs 39, 40) and TRIM33”
From TRIM33 switches off Ifnb1 gene transcription during the late phase of macrophage activation (2015) · cites this paper as [39]
There is limited understanding of the mechanisms that determine coactivator versus corepressor recruitment by RUNX1 and PU.1.
“There is limited understanding of the mechanisms that determine coactivator versus corepressor recruitment by RUNX1 and PU.1.17–20”
From RUNX1 regulates corepressor interactions of PU.1 (2011) · cites this paper as [18]
PU.1 can interact with coactivators or corepressors to function as either a transcriptional activator or a transcriptional repressor.
“PU.1 can interact with coactivators or corepressors to function as either a transcriptional activator or a transcriptional repressor.17–19”
From RUNX1 regulates corepressor interactions of PU.1 (2011) · cites this paper as [18]
The mechanisms that regulate corepressor versus coactivator interactions of RUNX1 and PU.1 are incompletely understood.
“However, the mechanisms that regulate corepressor versus coactivator interactions of RUNX1 and PU.1 are incompletely understood.17–20”
From RUNX1 regulates corepressor interactions of PU.1 (2011) · cites this paper as [18]
CBP stimulates PU.1 activity in transient transfections.
“and CBP stimulates PU.1 activity in transient trans- fections (82).”
From Inhibition of CBP-Mediated Protein Acetylation by the Ets Family Oncoprotein PU.1 (2002) · cites this paper as [82]

PU.1 is bifunctional: CBP binding activates PU.1 transcription, while TLE-4 supports PU.1-dependent repression.
“PU.1 is a bifunctional protein as for instance CBP binding leads to PU.1 transcriptional activation [47], whereas TLE-4 was found to support PU.1-dependent repres-sion [46].”
From PKCδ-Induced PU.1 Phosphorylation Promotes Hematopoietic Stem Cell Differentiation to Dendritic Cells (2011) · cites this paper as [47]
GST binding assays revealed that a portion of the transcriptional activation domain of PU.1 (amino acids 74-122) directly interacts with the region spanning residues 1283-1915 of CBP.
“GST binding assays revealed that a portion of the transcriptional activation domain of PU.1 (amino acids 74–122) directly interacts with the region spanning residues 1283–1915 of CBP (Fig. 4).”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [78]
CBP enhances PU.1-mediated transcription of multimerized PU-box luciferase reporter constructs, suggesting CBP acts as a co-activator for PU.1.
“CBP enhances PU.1-mediated transcription of multimerized PU-box luciferase reporter constructs, suggesting that CBP acts as a co-activator for the transcription factor PU.1.”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [78]
Because the amount of CBP is limited in cells, CBP may mediate positive and negative cross-talk between PU.1 and other transcription factors during haematopoietic cell differentiation.
“Because the amount of CBP is limited in cells, CBP may mediate positive and negative cross-talk between PU.1 and other transcription factors in the process of haematopoietic cell differentiation [78].”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [78]
In CV-1 cells, but not in NIH 3T3 cells, cooperation between Myb and C/EBP-α depended on the integrity of the PU.1-binding site.
“In CV-1 cells, but not in NIH 3T3 cells, cooperation between Myb and C/EBP-α depended on the integrity of the PU.1-binding site [78].”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [78]
CBP/p300 is a co-activator of PU.1 that binds to the transactivation domain of PU.1.
“One such candidate is CBP/p300, a co-activator of PU.1 [78], which binds to the transactivation domain of PU.1.”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [78]
Activation of EICE-dependent transcription may in part be due to recruitment of coactivator/histone acetylase CBP/p300, since CBP/p300 can interact with PU.1 but not ICSBP.
“This activation may in part be due to the recruitment of coactivator/ histone acetylase CBP/p300, since CBP/p300 can interact with PU.1 (but not ICSBP) (32, 59).”
From Gamma Interferon Triggers Interaction between ICSBP (IRF-8) and TEL, Recruiting the Histone Deacetylase HDAC3 to the Interferon-Responsive Element (2002) · cites this paper as [59]
This activation seems to involve other factors, notably the coactivator/histone acetylase CBP/p300, with which PU.1 is shown to interact.
“This activation seems to involve other factors, notably the coactivator/histone acetylase CBP/p300, with which PU.1 is shown to interact (59).”
From Gamma Interferon Triggers Interaction between ICSBP (IRF-8) and TEL, Recruiting the Histone Deacetylase HDAC3 to the Interferon-Responsive Element (2002) · cites this paper as [59]

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“1 can interact with the HAT CREB-binding protein (81).”
Background
Independent Repressor Domains in ZEB Regulate Muscle and T-Cell Differentiation
Postigo, A., & Dean, D. C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.7961 · Cited by 102 · see citing works
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 · see citing works
Eos, MITF, and PU.1 Recruit Corepressors to Osteoclast-Specific Genes in Committed Myeloid Progenitors
Hu, R., Sharma, S. M., Bronisz, A., Srinivasan, R., Sankar, U., & Ostrowski, M. C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01839-06 · Cited by 86 · see citing works
“Further, the N-terminal region of MITF (1-218) (MITF with aa 1 to 218), but not the C-terminal basic helix-loop-helixleucine zipper region (aa 219 to 419), formed a complex with GST-Eos (Fig.”
Background
Transcriptional Activation by STAT6 Requires the Direct Interaction with NCoA-1
Litterst, C. M., & Pfitzner, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108132200 · Cited by 83 · see citing works
Interleukin-3 Stimulation of mcl-1 Gene Transcription Involves Activation of the PU.1 Transcription Factor through a p38 Mitogen-Activated Protein Kinase-Dependent Pathway
Wang, J.-M., Lai, M.-Z., & Yang-Yen, H.-F. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.6.1896-1909.2003 · Cited by 83 · see citing works
Direct association between PU.1 and MeCP2 that recruits mSin3A-HDAC complex for PU.1-mediated transcriptional repression
Suzuki, M., Yamada, T., Kihara-Negishi, F., Sakurai, T., & Oikawa, T. (2003) · Oncogene · doi:10.1038/sj.onc.1207182 · Cited by 82 · see citing works
“In line with this, we have previously demonstrated that PU.1 interacts with CREB binding protein (CBP), which functions as a coactivator of transcription factors (Yamamoto et al., 1999).”
BackgroundMethodInfluentialSelf-citation
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 · see citing works
“1 and other transcription factors in the process of haematopoietic cell differentiation [78].”
Background
PU.1/Interferon Regulatory Factor Interactions; Mechanisms of Transcriptional Regulation
Marecki, S., & Fenton, M. J. (2000) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:33:2:127 · Cited by 74 · see citing works
“1 has been reported to interact with the histone acetylase CREB binding protein (CBP) (16), implicating PU.”
BackgroundInfluential
GATA‐2 and GATA‐2/ER display opposing activities in the development and differentiation of blood progenitors
Kitajima, K., Masuhara, M., Era, T., Enver, T., & Nakano, T. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf301 · Cited by 77 · see citing works
Cooperation of STAT-1 and IRF-1 in Interferon-γ-induced Transcription of the gp91 Gene
Kumatori, A., Yang, D., Suzuki, S., & Nakamura, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109803200 · Cited by 72 · see citing works
Inhibition of CBP-Mediated Protein Acetylation by the Ets Family Oncoprotein PU.1
Hong, W., Kim, A. Y., Ky, S., Rakowski, C., Seo, S.-B., Chakravarti, D., Atchison, M., & Blobel, G. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3729-3743.2002 · Cited by 71 · see citing works
“1 binds to the CH3 domain of CBP (82) (Fig.”
Background
TRIM33 switches off Ifnb1 gene transcription during the late phase of macrophage activation
Ferri, F., Parcelier, A., Petit, V., Gallouet, A.-S., Lewandowski, D., Dalloz, M., van den Heuvel, A., Kolovos, P., Soler, E., Squadrito, M. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms9900 · Cited by 71 · see citing works
A Review of Oxidative Stress Products and Related Genes in Early Alzheimer’s Disease
Cioffi, F., Adam, R. H. I., Bansal, R., & Broersen, K. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210497 · Cited by 73 · see citing works
CBP and p300: versatile coregulators with important roles in hematopoietic gene expression
Blobel, G. A. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.71.4.545 · Cited by 69 · see citing works
Gamma Interferon Triggers Interaction between ICSBP (IRF-8) and TEL, Recruiting the Histone Deacetylase HDAC3 to the Interferon-Responsive Element
Kuwata, T., Gongora, C., Kanno, Y., Sakaguchi, K., Tamura, T., Kanno, T., Basrur, V., Martinez, R., Appella, E., Golub, T., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.21.7439-7448.2002 · Cited by 69 · see citing works
Review: The Role of IRF-4 in Transcriptional Regulation
Marecki, S., & Fenton, M. J. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452737 · Cited by 67 · see citing works
“…loss of LPS-induced transcriptional activation, suggesting that phosphorylation of serine 148 is required for inducible transcriptional activation by LPS. Phos-MARECKI phorylation of other serine residues (41, 45, 132, and 133) is required at distinct events in myeloid development and maturation.”
Influential
Autocrine Induction of the Human Pro-IL-1β Gene Promoter by IL-1β in Monocytes
Toda, Y., Tsukada, J., Misago, M., Kominato, Y., Auron, P. E., & Tanaka, Y. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.168.4.1984 · Cited by 65 · see citing works
In vivo complex formation of PU.1 with HDAC1 associated with PU.1-mediated transcriptional repression
Kihara-Negishi, F., Yamamoto, H., Suzuki, M., Yamada, T., Sakurai, T., Tamura, T., & Oikawa, T. (2001) · Oncogene · doi:10.1038/sj.onc.1204756 · Cited by 65 · see citing works
“We have previously reported that PU.1 interacts with the coactivator CBP and the interaction has been implicated in transactivation (Yamamoto et al., 1999).”
BackgroundMethodResultInfluentialSelf-citation
Complex Formation of the Interferon (IFN) Consensus Sequence-binding Protein with IRF-1 Is Essential for Murine Macrophage IFN-γ-induced iNOS Gene Expression
Xiong, H., Zhu, C. Y., Li, H., Chen, F., Mayer, L., Ozato, K., Unkeless, J. C., & Plevy, S. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209583200 · Cited by 64 · see citing works
BSAP Can Repress Enhancer Activity by Targeting PU.1 Function
Maitra, S., & Atchison, M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.1911-1922.2000 · Cited by 72 · see citing works
RUNX1 regulates corepressor interactions of PU.1
Hu, Z., Gu, X., Baraoidan, K., Ibanez, V., Sharma, A., Kadkol, S., Munker, R., Ackerman, S., Nucifora, G., & Saunthararajah, Y. (2011) · Blood · doi:10.1182/blood-2010-10-312512 · Cited by 63 · see citing works
c-Jun Homodimers Can Function as a Context-Specific Coactivator
Grondin, B., Lefrançois, M., Tremblay, M., Saint-denis, M., Haman, A., Waga, K., Bédard, A., Tenen, D., & Hoang, T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00936-06 · Cited by 66 · see citing works
“Together with our observations of a more efficient recruitment of RNA Pol II, we propose that maximal assembly of PIC on the IL-1 promoter is achieved by multiple interactions and recruitment of TFIID and RNA Pol II holoenzymes containing Mediator complexes, CBP/p300, and some general transcription factors by the PU.1-”
Background
Yin Yang 1 enhancescyclooxygenase-2gene expression in macrophages
Joo, M., Wright, J. G., Hu, N. N., Sadikot, R. T., Park, G. Y., Blackwell, T. S., & Christman, J. W. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00474.2006 · Cited by 62 · see citing works
During ontogeny primitive (CD34+CD38−) hematopoietic cells show altered expression of a subset of genes associated with early cytokine and differentiation responses of their adult counterparts
Oh, I., Lau, A., & Eaves, C. J. (2000) · Blood · doi:10.1182/blood.v96.13.4160 · Cited by 63 · see citing works
Mutations of the PU.1 Ets domain are specifically associated with murine radiation-induced, but not human therapy-related, acute myeloid leukaemia
Suraweera, N., Meijne, E., Moody, J., Carvajal-Carmona, L. G., Yoshida, K., Pollard, P., Fitzgibbon, J., Riches, A., van Laar, T., Huiskamp, R., et al. (2005) · Oncogene · doi:10.1038/sj.onc.1208422 · Cited by 60 · see citing works
“…of the protein, this domain interacts with various proteins including GATA1 binding protein 1 (GATA1), CCAAT/enhancer binding protein beta (CEBPB), and other myeloid regulators such as c-jun and RUNX1/ AML-1 (Nagulapalli et al., 1995; Petrovick et al., 1998; Yamamoto et al., 1999).”
Background
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 56 · see citing works
Safeguard function of PU.1 shapes the inflammatory epigenome of neutrophils
Fischer, J., Walter, C., Tönges, A., Aleth, H., Jordão, M. J. C., Leddin, M., Gröning, V., Erdmann, T., Lenz, G., Roth, J., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0343-z · Cited by 56 · see citing works
Transcriptional Regulation of the Cyclooxygenase-2 Gene in Macrophages by PU.1
Joo, M., Park, G. Y., Wright, J. G., Blackwell, T. S., Atchison, M. L., & Christman, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306267200 · Cited by 55 · see citing works
Toll-like Receptor 2 and 4 (TLR2 and TLR4) Agonists Differentially Regulate Secretory Interleukin-1 Receptor Antagonist Gene Expression in Macrophages
Carl, V. S., Brown-Steinke, K., Nicklin, M. J. H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111847200 · Cited by 51 · see citing works
Functional polymorphism inALOX15results in increased allele-specific transcription in macrophages through binding of the transcription factor SPI1
Wittwer, J., Marti-Jaun, J., & Hersberger, M. (2005) · Human Mutation · doi:10.1002/humu.20273 · Cited by 50 · see citing works
“…protein [Hagemeier et al., 1993], the basal transcription factor TBP [Hagemeier et al., 1993], the transcriptional coactivators CBP/p300 [Yamamoto et al., 1999], the transcription factors GATA-1 and GATA-2 [Nerlov et al., 2000; Zhang et al., 1999], and the transcription factor NFEM5/Pip…”
Background
Epigenetic control of hematopoiesis: the PU.1 chromatin connection
van Riel, B., & Rosenbauer, F. (2014) · Biological Chemistry · doi:10.1515/hsz-2014-0195 · Cited by 47 · see citing works
Myeloblastin is an Myb target gene: mechanisms of regulation in myeloid leukemia cells growth-arrested by retinoic acid
Lutz, P. G., Houzel-Charavel, A., Moog‐Lutz, C., & Cayre, Y. E. (2001) · Blood · doi:10.1182/blood.v97.8.2449 · Cited by 49 · see citing works
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 · see citing works
PKCδ-Induced PU.1 Phosphorylation Promotes Hematopoietic Stem Cell Differentiation to Dendritic Cells
Hamdorf, M., Berger, A., Schüle, S., Reinhardt, J., & Flory, E. (2011) · Stem Cells · doi:10.1002/stem.564 · Cited by 45 · see citing works
5-Azacitidine in aggressive myelodysplastic syndromes regulates chromatin structure at PU.1 gene and cell differentiation capacity
Curik, N., Burda, P., Vargová, K., Pospíšil, V., Beličková, M., Vlckova, P., Savvulidi, F. G., Nečas, E., Hajkova, H., Haškovec, C., et al. (2012) · Leukemia · doi:10.1038/leu.2012.47 · Cited by 45 · see citing works
PML-Retinoic Acid Receptor α Inhibits PML IV Enhancement of PU.1-Induced C/EBPε Expression in Myeloid Differentiation
Yoshida, H., Ichikawa, H., Tagata, Y., Katsumoto, T., Ohnishi, K., Akao, Y., Naoe, T., Pandolfi, P. P., & Kitabayashi, I. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02422-06 · Cited by 45 · see citing works
“1 and p300/CBP can directly interact, at least in vitro (33); however, we found that their association is rather weak compared with those of other transcription factors such as AML1b.”
Background
c-Myb and Members of the c-Ets Family of Transcription Factors Act as Molecular Switches to Mediate Opposite Steroid Regulation of the Human Glucocorticoid Receptor 1A Promoter
Geng, C.-D., & Vedeckis, W. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508245200 · Cited by 43 · see citing works
PU.1 Suppresses Th2 Cytokine Expression via Silencing of GATA3 Transcription in Dendritic Cells
Yashiro, T., Kubo, M., Ogawa, H., Okumura, K., & Nishiyama, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137699 · Cited by 41 · see citing works
“1 is involved in chromatin remodeling by interaction with p300/CBP [12].”
Background
Disease-related potential of mutations in transcriptional cofactors CREB-binding protein and p300 in leukemias
Shigeno, K., Yoshida, H., Pan, L., Luo, J. M., Fujisawa, S., Naito, K., Nakamura, S., Shinjo, K., Takeshita, A., Ohno, R., et al. (2003) · Cancer Letters · doi:10.1016/s0304-3835(03)00442-7 · Cited by 42 · see citing works
Cooperative interaction between ETS1 and GFI1 transcription factors in the repression of Bax gene expression
Nakazawa, Y., Suzuki, M., Manabe, N., Yamada, T., Kihara‐Negishi, F., Sakurai, T., Tenen, D. G., Iwama, A., Mochizuki, M., & Oikawa, T. (2007) · Oncogene · doi:10.1038/sj.onc.1210140 · Cited by 39 · see citing works
“Cell extracts for Luc assays were prepared as described previously (Yamamoto et al., 1999).”
MethodInfluentialSelf-citation
Overlapping CRE and E Box Motifs in the Enhancer Sequences of the Bovine Leukemia Virus 5′ Long Terminal Repeat Are Critical for Basal and Acetylation-Dependent Transcriptional Activity of the Viral Promoter: Implications for Viral Latency
Calomme, C., Dekoninck, A., Nizet, S., Adam, E., Nguyên, T. L.-A., den Broeke, A. V., Willems, L., Kettmann, R., Burny, A., & Lint, C. M. V. (2004) · Journal of Virology · doi:10.1128/jvi.78.24.13848-13864.2004 · Cited by 39 · see citing works
“1/Spi-B (91, 92), USF2 (12), glucocorticoid receptor (38, 44), IRF1 (71), and IRF2 (56), have been shown to interact with acetyltransferases and/or to be acetylated.”
Background
The Essential Transcriptional Function of BRD4 in Acute Myeloid LeukemiaPreprint
Roe, J., & Vakoc, C. R. (2016) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2016.81.031039 · Cited by 39 · see citing works
Protein Acetylation Regulates Both PU.1 Transactivation and Igκ 3′ Enhancer Activity
Bai, Y., Srinivasan, L., Perkins, L., & Atchison, M. L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5160 · Cited by 38 · see citing works
ERM Transactivation Is Up-regulated by the Repression of DNA Binding after the PKA Phosphorylation of a Consensus Site at the Edge of the ETS Domain
Baert, J., Beaudoin, C., Coutte, L., & de Launoit, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107139200 · Cited by 37 · see citing works
Lineage switch induced by overexpression of Ets family transcription factor PU.1 in murine erythroleukemia cells
Yamada, T., Abe, M., Higashi, T., Yamamoto, H., Kihara‐Negishi, F., Sakurai, T., Shirai, T., & Oikawa, T. (2001) · Blood · doi:10.1182/blood.v97.8.2300 · Cited by 38 · see citing works
Self-citation
The transcription factor PU.1 mediates enhancer-promoter looping that is required for IL-1β eRNA and mRNA transcription in mouse melanoma and macrophage cell lines
Ha, S.-D., Cho, W., DeKoter, R. P., & Kim, S. O. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010149 · Cited by 35 · see citing works
Epigenetic Regulation during B Cell Differentiation Controls CIITA Promoter Accessibility
Green, M. R., Yoon, H., & Boss, J. M. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.6.3865 · Cited by 37 · see citing works
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 34 · see citing works
“Moreover, PU.1 has been shown to interact with chromatin-modifying enzymes: the histone acetyltransferase CREB binding protein (CBP) (Yamamoto et al., 1999) (which also interacts with Spi-B, Yamamoto et al., 2002) and the histone deacetylase HDAC1 (Kihara-Negishi et al., 2001), further implicating PU.1 in chromatin re…”
Background
The pioneer factor activity of c-Myb involves recruitment of p300 and induction of histone acetylation followed by acetylation-induced chromatin dissociation
Fuglerud, B. M., Ledsaak, M., Rogne, M., Eskeland, R., & Gabrielsen, O. S. (2018) · Epigenetics & Chromatin · doi:10.1186/s13072-018-0208-y · Cited by 34 · see citing works
Differential context-dependent effects of friend of GATA-1 (FOG-1) on mast-cell development and differentiation
Sugiyama, D., Tanaka, M., Kitajima, K., Zheng, J., Yen, H., Murotani, T., Yamatodani, A., & Nakano, T. (2007) · Blood · doi:10.1182/blood-2007-08-104489 · Cited by 32 · see citing works
Spi-1/PU.1 Oncoprotein Affects Splicing Decisions in a Promoter Binding-dependent Manner
Guillouf, C., Gallais, I., & Moreau-Gachelin, F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512049200 · Cited by 30 · see citing works
Expression of Adipose Differentiation-Related Protein (ADRP) Is Conjointly Regulated by PU.1 and AP-1 in Macrophages
Wei, P. Y., Taniguchi, S., Sakai, Y., Imamura, M., Inoguchi, T., Nawata, H., Oda, S., Nakabeppu, Y., Nishimura, J., & Ikuyama, S. (2005) · The Journal of Biochemistry · doi:10.1093/jb/mvi136 · Cited by 28 · see citing works
Multiple functional domains of the oncoproteins Spi-1/PU.1 and TLS are involved in their opposite splicing effects in erythroleukemic cells
Delva, L., Gallais, I., Guillouf, C., Denis, N., Orvain, C., & Moreau-Gachelin, F. (2004) · Oncogene · doi:10.1038/sj.onc.1207578 · Cited by 26 · see citing works
“Some of these proteins are ubiquitous factors such as the basal transcription factor TFIID (Hagemeier et al., 1993) and the co-activator/integrator CBP (Yamamoto et al., 1999).”
Background
Transcriptional Regulation of the p67 Gene
Li, S.-L., Valente, A. J., Wang, L., Gamez, M. J., & Clark, R. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106111200 · Cited by 27 · see citing works
Modeling the Hematopoietic Landscape
Brown, G., & Ceredig, R. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00104 · Cited by 25 · see citing works
“1 binds the histone acetyltransferases CREB-binding protein and p300 (Yamamoto et al., 1999; Bai et al., 2005) and a histone deacetylase complex consisting of histone deacetylase 1 and mammalian Sin3a (Kihara-Negishi et al.”
Background
AP-1 is essential for p67phoxpromoter activity
Gauss, K. A., Bunger, P. L., & Quinn, M. T. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.71.1.163 · Cited by 25 · see citing works
Structural mechanism of synergistic targeting of the CX3CR1 nucleosome by PU.1 and C/EBPα
Lian, T., Guan, R., Zhou, B., & Bai, Y. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01189-z · Cited by 26 · see citing works
“The N-terminal regions of both PU.1 and C/EBPα interact with basal transcription factors such as TFIID, TFIIB and TBP 28,29 , histone acetyltransferases CREB-binding protein (CBP) 30,31 , as well as SWI/SNF chromatin remodelers 29,32 .”
Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb.
Yamamoto, H., Kihara‐Negishi, F., Yamada, T., Suzuki, M., Nakano, T., & Oikawa, T. (2002) · PubMed · Cited by 24 · see citing works
Self-citation
Bisphenol A significantly enhances the neutrophilic differentiation of promyelocytic HL-60 cells
Watanabe, H., Adachi, R., Kusui, K., Hirayama, A., Kasahara, T., & Suzuki, K. (2003) · International Immunopharmacology · doi:10.1016/s1567-5769(03)00182-6 · Cited by 23 · see citing works
An intron GATA‐binding site regulates chromatin accessibility and is essential for IL‐4 gene expression in mast cells
Kwan, M., Powell, D. R., Nachman, T. Y., & Brown, M. A. (2005) · European Journal of Immunology · doi:10.1002/eji.200425619 · Cited by 22 · see citing works
Conserved ETS Domain Arginines Mediate DNA Binding, Nuclear Localization, and a Novel Mode of bZIP Interaction
Listman, J. A., Wara-aswapati, N., Race, J. E., Blystone, L. W., Walker‐Kopp, N., Yang, Z., & Auron, P. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509143200 · Cited by 21 · see citing works
PU.1 Regulates Positive Regulatory Domain I-Binding Factor 1/Blimp-1 Transcription in Lymphoma Cells
Desai, S., Bolick, S. C. E., Maurin, M. M., & Wright, K. L. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901120 · Cited by 21 · see citing works
Context-dependent Pax-5 repression of a PU.1/NF-κB regulated reporter gene in B lineage cells
Linderson, Y., French, N. S., Neurath, M. F., & Pettersson, S. (2001) · Gene · doi:10.1016/s0378-1119(00)00546-1 · Cited by 19 · see citing works
Pub, a novel PU.1 binding protein, regulates the transcriptional activity of PU.1
Hirose, S., Nishizumi, H., & Sakano, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.212 · Cited by 18 · see citing works
Molecular basis of Stat1 and PU.1 cooperation in cytokine-induced Fc receptor I promoter activation
Aittomäki, S. (2004) · International Immunology · doi:10.1093/intimm/dxh037 · Cited by 18 · see citing works
Deacetylase Inhibitors and the Viral Transactivator TaxBLV Synergistically Activate Bovine Leukemia Virus Gene Expression via a cAMP-responsive Element- and cAMP-responsive Element-binding Protein-dependent Mechanism
Nguyên, T. L.-A., Calomme, C., Wijmeersch, G., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404081200 · Cited by 16 · see citing works
EID3 directly associates with DNMT3A during transdifferentiation of human umbilical cord mesenchymal stem cells to NPC-like cells
Luo, L., Chen, W., Yin, J. Q., & Xu, R. (2017) · Scientific Reports · doi:10.1038/srep40463 · Cited by 16 · see citing works
SPI-C and STAT6 can cooperate to stimulate IgE germline transcription
Carlsson, R., Thorell, K., Liberg, D., & Leanderson, T. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.026 · Cited by 15 · see citing works
Retinoic acid triggers c-kit gene expression in spermatogonial stem cells through an enhanceosome constituted between transcription factor binding sites for retinoic acid response element (RARE), spleen focus forming virus proviral integration oncogene (SPFI1) (PU.1) and E26 transformation-specific (ETS)
Koli, S., Mukherjee, A., & Reddy, K. V. R. (2015) · Reproduction Fertility and Development · doi:10.1071/rd15145 · Cited by 14 · see citing works
Recent insights into the biology of Hodgkin lymphoma: unraveling the mysteries of the Reed–Sternberg cell
Roullet, M. R., & Bagg, A. (2007) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.7.6.805 · Cited by 14 · see citing works
Impaired repressor activity and biological functions of PU.1 in MEL cells induced by mutations in the acetylation motifs within the ETS domain
Kihara-Negishi, F., Suzuki, M., Yamada, T., Sakurai, T., & Oikawa, T. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.098 · Cited by 13 · see citing works
Self-citation
Effects of PU.1-induced mouse calcium–calmodulin-dependent kinase I-like kinase (CKLiK) on apoptosis of murine erythroleukemia cells
Yamada, T., Suzuki, M., Satoh, H., Kihara‐Negishi, F., Nakano, H., & Oikawa, T. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.023 · Cited by 13 · see citing works
Self-citation
Distinct functions for signal transducer and activator of transcription 1 and PU.1 in transcriptional activation of Fc γ receptor I promoter
Aittomäki, S., Yang, J., Scott, E. W., Simon, M. C., & Silvennoinen, O. (2002) · Blood · doi:10.1182/blood-2001-12-0236 · Cited by 13 · see citing works
Interaction between the homeodomain protein HOXC13 and ETS family transcription factor PU.1 and its implication in the differentiation of murine erythroleukemia cells
Yamada, T., Shimizu, T., Suzuki, M., Kihara‐Negishi, F., Nanashima, N., Sakurai, T., Yang, F., Akita, M., Oikawa, T., & Tsuchida, S. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.11.005 · Cited by 11 · see citing works
Self-citation
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Protein inhibitor of activated STAT1 (PIAS1) inhibits IRF8 activation of Epstein-Barr virus lytic gene expression
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“1 also interacts with CRE-binding protein (CBP) or p300 and functions as a coactivator for several other transcription factors (Yamamoto et al., 1999).”
Background
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BackgroundInfluential
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Authors: Yamamoto, H., Kihara-Negishi, F., Yamada, T., Hashimoto, Y., & Oikawa, T.
Affiliations: Sasaki Institute (JP)
ORCID: Yamada, Toshiyuki
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 1999-02-18
Volume: 18
Issue: 7
Pages: 1495-1501
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1202427
OpenAlex: W2318149005
Semantic Scholar: b28b07fc5cb5ab0b001e5a4822b86f270638d7f1
Cited by: 111
References: 49
Citations by year: 2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2021: 1 · 2019: 5 · 2018: 2 · 2017: 2 · 2016: 2 · 2015: 5 · 2014: 1 · 2013: 1 · 2012: 1
FWCI: 3.54
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Health Sciences › Medicine › Hematology › Hematopoietic Stem Cell Transplantation
Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Keywords: PU.1, CREB-binding protein, CBP, transcriptional coactivator, ETS transcription factors, protein-protein interaction, transactivation domain, transcriptional activation
MeSH terms: Proto-Oncogene Protein Spi-1, Animals, Nuclear Proteins, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Trans-Activators

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Physical and functional interactions between the transcription factor PU.1 and the coactivator CBP

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