The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Effect of PU.1 phosphorylation on interaction with NF-EM5 and transcriptional activation
Abstract
PU.1 recruits the binding of a second B cell-restricted nuclear factor, NF-EM5, to a DNA site in the immunoglobulin kappa 3' enhancer. DNA binding by NF-EM5 requires a protein-protein interaction with PU.1 and specific DNA contacts. Dephosphorylated PU.1 bound to DNA but did not interact with NF-EM5. Analysis of serine-to-alanine mutations in PU.1 indicated that serine 148 (Ser148) is required for protein-protein interaction. PU.1 produced in bacteria did not interact with NF-EM5. Phosphorylation of bacterially produced PU.1 by purified casein kinase II modified it to a form that interacted with NF-EM5 and that recruited NF-EM5 to bind to DNA. Phosphopeptide analysis of bacterially produced PU.1 suggested that Ser148 is phosphorylated by casein kinase II. This site is also phosphorylated in vivo. Expression of wild-type PU.1 increased expression of a reporter construct containing the PU.1 and NF-EM5 binding sites nearly sixfold, whereas the Ser148 mutant form only weakly activated transcription. These results demonstrate that phosphorylation of PU.1 at Ser148 is necessary for interaction with NF-EM5 and suggest that this phosphorylation can regulate transcriptional activity.
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In the citing paper
“In each instance, the binding of Pip to DNA is dependent on DNA-bound PU.1, which must be phosphorylated on Ser148 (pSer148; Pongubala et al., 1993).”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Pongubala et al., 1993
In the citing paper
“More-over, the ETS domain factor PU.1, in particular, can be phosphorylated by casein kinase (53,65) or JNK in vitro (66)”
From c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription Factor (1999) · cites this paper as [53]
In the citing paper
“Phosphorylation of PU.1 at Ser-148 is necessary for interaction with NF-EM5 (53) or stimulation by lipopolysaccharide (65)”
From c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription Factor (1999) · cites this paper as [53]
In the citing paper
“and the activity of PU.1 is known to be regulated by phosphorylation (53,54,65).”
From c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription Factor (1999) · cites this paper as [53]
In the citing paper
“casein kinase II has been suggested to be responsible for phosphorylation of PU.1 at serine 148 (27, 35)”
In the citing paper
“a serine phosphorylation at position 148 in the proline-, glutamic-acid-, serine-, and threonine-rich domain mediates the interaction between PU.1 and the B-cell enhancer factor (NF-EM5).”
In the citing paper
“phosphorylation at serine 148 is required for its interaction with a B-cell-restricted transcription factor, PIP (NF-EM5), and activates the immunoglobulin κ 3′ enhancer (35).”
In the citing paper
“PU.1 is a phosphoprotein”
In the citing paper
“Previous studies have demonstrated that phosphorylation of PU.1 at position 148 is necessary for recruitment of PIP to the κE3′-enhancer.”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“Transcriptional activity of the enhancer is greatly reduced in the presence of a PU.1 mutant containing a serine to alanine mutation at position 148 apparently because of the inability of PU.1 S148A to recruit PIP to its adjacent DNA-binding site (22”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“Previous studies have demonstrated that transcriptional activity of the κE3′-enhancer is critically dependent on binding components of the κE3′-CRE (binds c-Fos, c-Jun, CREM, and ATF1), PU.1 plus PIP (binds PU.1 and PIP) and E2A (binds E12/47) sites.”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“Within the κE3′-enhancer, PU.1 recruits the binding of PIP, through protein-protein interaction to its adjacent DNA-binding site (22”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“Mutation of any one of these binding sites greatly reduces enhancer activity (22-25”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“This interaction is important for the transcriptional activity of the κE3′-enhancer (22”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“Previous studies demonstrated that PU.1 recruits the binding of PIP through phosphorylation-dependent interaction with PU.1 at Ser148.”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [23]
In the citing paper
“This domain interacts with interferon regulatory factors (IRFs), including Pip/NF-EM5 and interferon consensus sequence binding protein (ICSBP) [44–46].”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [44]
In the citing paper
“Similar ICSBP protein-protein interactions are necessary for activation of the TOLL-like receptor 4 gene in mature monocytes (22).”
Citations
Cites
CREB: a Ca 2+ -Regulated Transcription Factor Phosphorylated by Calmodulin-Dependent Kinases
Sheng, M., Thompson, M. A., & Greenberg, M. E. (1991) · Science · doi:10.1126/science.1646483 · Cited by 1,498
Phosphorylation of c-jun mediated by MAP kinases
Pulverer, B., Kyriakis, J. M., Avruch, J., Nikolakaki, E., & Woodgett, J. R. (1991) · Nature · doi:10.1038/353670a0 · Cited by 1,470
Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB
Yamamoto, K. K., Gonzalez, G. A., Biggs, W., & Montminy, M. (1988) · Nature · doi:10.1038/334494a0 · Cited by 1,281
Affinity purification of sequence-specific DNA binding proteins.
Kadonaga, J. T., & Tjian, R. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.16.5889 · Cited by 1,154
Activation in vitro of NF-κB" by phosphorylation of its inhibitor IκB"
Ghosh, S., & Baltimore, D. (1990) · Nature · doi:10.1038/344678a0 · Cited by 1,150
[42] Detection and quantification of phosphotyrosine in proteins
Cooper, J. A., Sefton, B. M., & Hunter, T. R. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99075-4 · Cited by 1,109
Singh, H., Sen, R., Baltimore, D., & Sharp, P. A. (1986) · Nature · doi:10.1038/319154a0 · Cited by 1,087
Boyle, W. J., Smeal, T., Defize, L. H. K., Angel, P. E., Woodgett, J. R., Karin, M., & Hunter, T. R. (1991) · Cell · doi:10.1016/0092-8674(91)90241-p · Cited by 1,039
The macrophage and B cell-specific transcription factor PU.1 is related to the ets oncogene
Klemsz, M. J., McKercher, S. R., Celada, A., Van Beveren, C., & Maki, R. A. (1990) · Cell · doi:10.1016/0092-8674(90)90219-5 · Cited by 954
Self-citationGrosschedl, R., & Baltimore, D. (1985) · Cell · doi:10.1016/s0092-8674(85)80069-6 · Cited by 520
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IRF Family of Transcription Factors as Regulators of Host Defense
Taniguchi, T., Ogasawara, K., Takaoka, A., & Tanaka, N. (2001) · Annual Review of Immunology · doi:10.1146/annurev.immunol.19.1.623 · Cited by 1,658
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
Self-citationThe ETS-domain transcription factor family
Sharrocks, A. D. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35099076 · Cited by 1,086
Molecular biology of the Ets family of transcription factors
Oikawa, T., & Yamada, T. (2003) · Gene · doi:10.1016/s0378-1119(02)01156-3 · Cited by 701
Transcription Factors, Normal Myeloid Development, and Leukemia
Tenen, D. G., Hromas, R., Licht, J. D., & Zhang, D.-E. (1997) · Blood · doi:10.1182/blood.v90.2.489 · Cited by 735
The transcriptional control of hematopoiesis [see comments]
Shivdasani, R., & Orkin, S. (1996) · Blood · doi:10.1182/blood.v87.10.4025.bloodjournal87104025 · Cited by 560
Giese, K., Kingsley, C., Kirshner, J. R., & Grosschedl, R. (1995) · Genes & Development · doi:10.1101/gad.9.8.995 · Cited by 541
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
Wang, D., Westerheide, S. D., Ostrander, J. H., & Baldwin, A. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001358200 · Cited by 454
Pathogenesis of Human B Cell Lymphomas
Shaffer, A. L., Young, R. M., & Staudt, L. M. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-020711-075027 · Cited by 457
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
“In addition, in contrast to the case in B cells (25), we were unable to detect any significant effect of a serine-toalanine mutation at position 148 (or at positions 41, 45, 132, and 133) (kindly provided by M.”
Ets target genes: past, present and future
Sementchenko, V. I., & Watson, D. K. (2000) · Oncogene · doi:10.1038/sj.onc.1204034 · Cited by 371
Regulatory Mechanisms that Determine the Development and Function of Plasma Cells
Calame, K. L., Lin, K., & Tunyaplin, C. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141138 · Cited by 380
Specificity within the ets Family of Transcription Factors
(1998) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60738-1 · Cited by 344
Macián, F., García‐Rodríguez, C., & Rao, A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4783 · Cited by 329
The ETS-domain transcription factor family
Sharrocks, A. D., Brown, A. L., Ling, Y., & Yates, P. R. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(97)00086-1 · Cited by 317
Hohaus, S., Petrovick, M. S., Voso, M. T., Sun, Z., Zhang, D.-E., & Tenen, D. G. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.10.5830 · Cited by 284
“NF-EM5 (47), did not abolish the ability of PU.1 to form PU-SF (Fig.”
BackgroundResultInfluentialSignal integration between IFNγ and TLR signalling pathways in macrophages
Schroder, K., Sweet, M. J., & Hume, D. A. (2006) · Immunobiology · doi:10.1016/j.imbio.2006.05.007 · Cited by 288
Johannsen, E., Koh, E., Mosialos, G., Tong, X., Kieff, E. D., & Grossman, S. R. (1995) · Journal of Virology · doi:10.1128/jvi.69.1.253-262.1995 · Cited by 250
“1–NF-EM5 complex [36]), LBF4 was purified from IB4 cell nuclear extracts by sequential cation exchange, DNAcellulose, and sequence-specific DNA affinity chromatography, using EMSA to monitor LBF4 activity.”
MethodBrass, A. L., Kehrli, E., Eisenbeis, C. F., Storb, U., & Singh, H. (1996) · Genes & Development · doi:10.1101/gad.10.18.2335 · Cited by 242
Heterozygous PU.1 mutations are associated with acute myeloid leukemia
Mueller, B. U., Pabst, T., Osato, M., Asou, N., Johansen, L. M., Minden, M. D., Behre, G., Hiddemann, W., Ito, Y., & Tenen, D. G. (2002) · Blood · doi:10.1182/blood.v100.3.998 · Cited by 243
Multiple Functional Domains of AML1: PU.1 and C/EBPα Synergize with Different Regions of AML1
Petrovick, M. S., Hiebert, S. W., Friedman, A. D., Hetherington, C. J., Tenen, D. G., & Zhang, D.-E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3915 · Cited by 218
“mAML1A(1-288) is terminated at amino acid 288 of AML1A.”
BackgroundMethodInfluentialHematopoietic lineage- and stage-restricted expression of the ETS oncogene family member PU.1
Hromas, R., Orazi, A., Neiman, R., Maki, R., Van Beveran, C., Moore, J., & Klemsz, M. (1993) · Blood · doi:10.1182/blood.v82.10.2998.2998 · Cited by 216
Self-citationTranscription factors that regulate monocyte/macrophage differentiation
Valledor, A. F., Borràs, F. E., Cullell-Young, M., & Celada, A. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.63.4.405 · Cited by 215
“1 with other proteins in B cells [11, 12]; (3) the DNA-binding domain, also known as the ets domain, which is a consensus motif present in all the ets family members [13].”
BackgroundRegulation of interleukin-12 production in antigen-presenting cells
Mal, X., & Trinchieri, G. (2001) · Advances in immunology · doi:10.1016/s0065-2776(01)79002-5 · Cited by 213
Lieschke, G. J., Oates, A. C., Paw, B. H., Thompson, M. A., Hall, N. E., Ward, A. C., Ho, R. K., Zon, L. I., & Layton, J. E. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0657 · Cited by 183
Brass, A. L., Zhu, A. Q., & Singh, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.4.977 · Cited by 204
“Formation of the PU.1– Pip protein adduct was dependent on: (i) phosphorylation of Ser148 in PU.1; (ii) Lys399 in Pip’s interaction helix; and (iii) λB DNA containing intact PU.1- and Pip-binding sites (Figure 5B, lanes 3–8, probes designated B1 and B2 contain severe mutations in either the PU.1- or Pip-binding sites;…”
BackgroundInfluentialGene regulation by Ets proteins
Janknecht, R. (1993) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(93)90014-4 · Cited by 194
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
“1 is a transcriptional activator whose function is modulated by the DNA sequence of its binding site, by posttranslational processing like phosphorylation (47), and by direct interaction with other nuclear proteins (13, 46).”
BackgroundA direct physical association between ETS and AP-1 transcription factors in normal human T cells
Bassuk, A. G., & Leiden, J. M. (1995) · Immunity · doi:10.1016/1074-7613(95)90092-6 · Cited by 186
Liu, J., Cao, S., Kim, S. J., Chung, E. Y., Homma, Y., Guan, X., Jimenez, V., & Ma, X. (2005) · Current Immunology Reviews · doi:10.2174/1573395054065115 · Cited by 189
“1 belongs to the ets family of DNA binding proteins [177,178].”
BackgroundIRF4: Immunity. Malignancy! Therapy?
Shaffer, A. L., Emre, N. C. T., Romesser, P. B., & Staudt, L. M. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1845 · Cited by 197
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
Eisenbeis, C. F., Singh, H., & Storb, U. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.10.6452 · Cited by 182
Tootle, T. L., & Rebay, I. (2005) · BioEssays · doi:10.1002/bies.20198 · Cited by 184
“1 (Spi-1) Casein kinase II Potentiates protein–protein interactions, increases activation (130)”
BackgroundEklund, E. A., Jalava, A., & Kakar, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13957 · Cited by 176
Potential Autoregulation of Transcription Factor PU.1 by an Upstream Regulatory Element
Okuno, Y., Huang, G., Rosenbauer, F., Evans, E. K., Radomska, H. S., Iwasaki, H., Akashi, K., Moreau-Gachelin, F., Li, Y., Zhang, P., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2832-2845.2005 · Cited by 174
“In addition, PU.1 controls gene expression by interacting with many factors such as c-Jun (7), IRF4/Pip (14, 46, 47), NF-interleukin 6 beta (IL-6 ) (C/EBP ) (36), C/EBP (51), and GATA-1 (38, 52,”
Casein kinase II in signal transduction and cell cycle regulation
Litchfield, D. W., & L�scher, B. (1993) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076770 · Cited by 176
EWS/Fli-1 chimeric protein is a transcriptional activator.
Ohno, T., Rao, V. N., & Reddy, E. S. (1993) · PubMed · Cited by 167
ETS transcription factors and regulation of immunity
Gallant, S., & Gilkeson, G. S. (2006) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-006-0017-z · Cited by 165
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
“1 in lymphocytes include the Ig K light chain gene 3' enhancer (8, 9), the Ig k 2-4 enhancer (10), the Ig heavy chain p, en-”
BackgroundSelf-citationFisher, R. C., & Scott, E. W. (1998) · STEM CELLS · doi:10.1002/stem.160025 · Cited by 158
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
“The peptide consisting of amino acids 118 to 160 has been demonstrated, when phosphorylated at S-148, to bind factor NF-EM5, which is essential for the function of the Igk and Igl gene downstream enhancers (9, 27, 28).”
BackgroundHwang, E. S., Hong, J., & Glimcher, L. H. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051044 · Cited by 166
“For example, serine phosphorylation of UBF is required for its interaction with RNA polymerase 1 (67), PU.1 phosphorylation regulates its interaction with NF-EM5 (68) and the dimerization of IRF-3 and -7 is activated by phosphorylation of their COOH-terminal domains by the IKK kinase complex (69).”
BackgroundMeraro, 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
Self-citationThe key role of PU.1/SPI-1 in B cells, myeloid cells and macrophages
Lloberas, J., Soler, C., & Celada, A. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01442-5 · Cited by 142
Shore, P., & Sharrocks, A. D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.5.3283 · Cited by 145
The diverse roles of IRF4 in late germinal center B‐cell differentiation
Silva, N. S. D., Simonetti, G., Heise, N., & Klein, U. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01113.x · Cited by 154
Sol, V. V., Punzón, C., & Fresno, M. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.7.4461 · Cited by 138
“1 is a transcription factor of the Ets family (49), which has been described as an important partner of IRF-1 and/or IRF-8 in the transcriptional regulation of several genes, such as IL-1 or NADPH phagocyte oxidase (21, 22).”
BackgroundFord, A. M., Bennett, C. L., Healy, L. E., Towatari, M., Greaves, M. F., & Enver, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10838 · Cited by 136
Ma, X., Neurath, M. F., Gri, G., & Trinchieri, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10389 · Cited by 137
TRANSCRIPTIONAL REGULATION DURING B CELL DEVELOPMENT
Henderson, A. J., & Calame, K. L. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.163 · Cited by 140
Laux, G., Adam, B.-L., Strobl, L. J., & Moreau-Gachelin, F. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06900.x · Cited by 139
ISGF3γ p48, a specificity switch for interferon activated transcription factors
Bluyssen, H. A. R. (1996) · Cytokine & Growth Factor Reviews · doi:10.1016/1359-6101(96)00005-6 · Cited by 135
Regulation of granulopoiesis by transcription factors and cytokine signals
Ward, A. C., Loeb, D., Soede-Bobok, A. A., Touw, I., & Friedman, A. (2000) · Leukemia · doi:10.1038/sj.leu.2401808 · Cited by 134
Lineage-Specific Modulation of Interleukin 4 Signaling by Interferon Regulatory Factor 4
Gupta, S. K., Jiang, M., Anthony, A., & Pernis, A. B. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1837 · 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
“78 LPS has been shown to induce PU.1 phosphorylation via casein kinase II (CKII) in macrophages.”
Fisher, R. J., Fivash, M. J., Casas‐Finet, J. R., Erickson, J. W., Kondoh, A., Bladen, S. V., Fisher, C. L., Watson, D. K., & Papas, T. S. (1994) · Protein Science · doi:10.1002/pro.5560030210 · Cited by 127
Shin, M. K., & Koshland, M. E. (1993) · Genes & Development · doi:10.1101/gad.7.10.2006 · Cited by 126
Reddy, M. A., Yang, B. S., Yue, X., Barnett, C. J., Ross, I. L., Sweet, M. J., Hume, D. A., & Ostrowski, M. C. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.6.2309 · Cited by 123
“1 mediate tissue-specific expression of genes in hematopoietic cell types (9-12), in combination with other transcription factors such as the immunoglobulin-enhancer binding factor NF-EM5 (13).”
BackgroundEichbaum, Q. G., Iyer, R., Raveh, D. P., Mathieu, C., & Ezekowitz, R. A. (1994) · The Journal of experimental medicine · doi:10.1084/jem.179.6.1985 · Cited by 86
Bradford, A. P., Conrad, K. E., Wasylyk, C., Wasylyk, B., & Gutierrez‐Hartmann, A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.5.2849 · Cited by 114
“1 phosphorylation (68); (ii) Elf-1 interacts only with dephosphorylated forms of Rb (81); and (iii) Elk-1 and serum response factor interact directly and in the absence of the composite DNA-binding site (75).”
BackgroundInfluentialThe Role of Ets Transcription Factors in the Development and Function of the Mammalian Immune System
Bassuk, A. G., & Leiden, J. M. (1997) · Advances in immunology · doi:10.1016/s0065-2776(08)60887-1 · Cited by 110
Fletcher, J. C., & Thummel, C. S. (1995) · Development · doi:10.1242/dev.121.5.1411 · Cited by 114
Modulation of T Cell Cytokine Production by Interferon Regulatory Factor-4
Hu, C.-M., Jang, S. Y., Fanzo, J., & Pernis, A. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205895200 · 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
“PU.1 has been reported to interact with retinoblastoma protein (Rb) and TFIID through the N-terminal region (1 ± 75 aa) (Hagemeier et al., 1993), NF-EM5/Pip through the PEST domain (119 ± 160 aa) (Eisenbeis et al., 1995) and NF-IL6b through the Ets domain (245 ± 272 aa) (Nagulapalli et al., 1995).”
BackgroundMarecki, 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
“1, IRF-1, and IRF-2 can interact with IRF-4 and ICSBP via their PEST domains (23, 29, 42).”
Oikawa, T., Yamada, T., Kihara-Negishi, F., Yamamoto, H., Kondoh, N., Hitomi, Y., & Hashimoto, Y. (1999) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400534 · Cited by 109
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
Jurutka, P. W., Hsieh, J., Nakajima, S., Haussler, C. A., Whitfield, G. K., & Haussler, M. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3519 · Cited by 104
Isolation of two E-box binding factors that interact with the rat tyrosine hydroxylase enhancer
Yoon, S. O., & Chikaraishi, D. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32330-x · Cited by 104
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
Zhao, B., & Sample, C. E. (2000) · Journal of Virology · doi:10.1128/jvi.74.11.5151-5160.2000 · Cited by 107
“GST fusion proteins that contained full-length Spi-1 (GST-Spi-1), the amino-terminal activation domain [GST-Spi-1 N (1-90)], or the C-terminal ets domain of either Spi-1 [GST-Spi-1 ets (90-264)] or Spi-B [GST-Spi-B ets (121-262)] were generated.”
BackgroundCD18 (beta 2 leukocyte integrin) promoter requires PU.1 transcription factor for myeloid activity.
Rosmarin, A. G., Caprio, D. G., Levy, R., & Simkevich, C. P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.801 · Cited by 94
The Transcription Factor PU.1 is a Critical Regulator of Cellular Communication in the Immune System
Turkistany, S. A., & DeKoter, R. P. (2011) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-011-0147-9 · Cited by 96
Biosynthesis of casein kinase II in lymphoid cell lines
Lüscher, B., & Litchfield, D. W. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18651.x · Cited by 99
Suppression of IL-12 Transcription in Macrophages Following Fcγ Receptor Ligation
Cappiello, M. G., Sutterwala, F. S., Trinchieri, G., Mosser, D. M., & Ma, X. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.7.4498 · Cited by 98
“1 belongs to the Ets family of DNA binding proteins (25, 26).”
BackgroundA compilation of composite regulatory elements affecting gene transcription in vertebrates
Kel, O. V., Romaschenko, A. G., Kel, A. E., Wingender, E., & Kolchanov, N. A. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.20.4097 · Cited by 99
Activation of Transcription by PU.1 Requires both Acidic and Glutamine Domains
Klemsz, M. J., & Maki, R. A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.1.390 · Cited by 93
“These include the kappa (30, 31) and lambda (7) lightchain, heavy-chain (27, 34), J chain (36), and B29 (28) genes in B cells and the CD11b (29), macrophage colony-stimulating factor receptor (37), scavenger receptor (26), FcgRIIIA (8), FcgR1b (6), and interleukin 1b (22) genes in macrophages.”
BackgroundSelf-citationBeuten, J., Gelfond, J., Franke, J. L., Weldon, K. S., Crandall, A. C., Johnson‐Pais, T. L., Thompson, I. M., & Leach, R. J. (2009) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-09-0076 · Cited by 95
The zebrafish spi1 promoter drives myeloid-specific expression in stable transgenic fish
Ward, A. C., McPhee, D., Condron, M. M., Varma, S., Cody, S. H., Onnebo, S. M. N., Paw, B. H., Zon, L. I., & Lieschke, G. J. (2003) · Blood · doi:10.1182/blood-2003-03-0966 · Cited by 94
Calcium-induced phosphorylation of ETS1 inhibits its specific DNA binding activity.
Rabault, B., & Ghysdael, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46906-2 · Cited by 94
The RUNX1–PU.1 axis in the control of hematopoiesis
Imperato, M. R., Cauchy, P., Obier, N., & Bonifer, C. (2015) · International Journal of Hematology · doi:10.1007/s12185-015-1762-8 · Cited by 94
“Phosphorylation of a central serine residue in position 148 has been found to be responsible for protein–protein interactions, which are also decisive in the control of transcriptional activity [22].”
BackgroundNF-κB Down-regulates Expression of the B-lymphoma Marker CD10 through a miR-155/PU.1 Pathway
Thompson, R. C., Herscovitch, M., Zhao, I., Ford, T. J., & Gilmore, T. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177063 · Cited by 91
The Human β2 Integrin CD18 promoter consists of Two Inverted Ets cis Elements
Böttinger, E. P., Shelley, C. S., Farokhzad, O. C., & Arnaout, M. A. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.4.2604 · Cited by 89
Yamada, T., Kondoh, N., Matsumoto, M., Yoshida, M., Maekawa, A., & Oikawa, T. (1997) · Blood · doi:10.1182/blood.v89.4.1383 · Cited by 87
Becker, C., Wirtz, S. J., Ma, X., Blessing, M., Galle, P. R., & Neurath, M. F. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.5.2608 · Cited by 89
Perez, C., Coeffier, E., Moreau-Gachelin, F., Wietzerbin, J., & Benech, P. D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5023 · Cited by 84
Feinman, R., Qiu, W. Q., Pearse, R. N., Nikolajczyk, B. S., Sen, R., Sheffery, M., & Ravetch, J. V. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06696.x · Cited by 88
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
Self-citationMarecki, S., Atchison, M. L., & Fenton, M. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2713 · Cited by 87
Self-citationMoulton, K. S., Semple, K., Wu, H., & Glass, C. K. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4408 · Cited by 86
“1-NF-EM5 interaction was shown to be regulated by a phosphorylation event at serine 148 that is necessary for efficient transcriptional activation of the kappa 3' enhancer sequence (25).”
BackgroundStütz, A. M., & Woisetschläger, M. (1999) · PubMed · Cited by 86
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
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 90
“PU.1 was shown to interact with many transcription factors or coactivators, including NF-EM5, Ets-1, NF-IL-6, HMG-I(Y), c-Jun, IRF-1, ICSBP, AML1, and CBP (2, 8, 25, 33, 35, 36, 51, 52).”
BackgroundInfluentialRegulation of Immunoglobulin Light Chain Isotype Expression
Gorman, J. R., & Alt, F. W. (1998) · Advances in immunology · doi:10.1016/s0065-2776(08)60607-0 · Cited by 82
Do lampreys have lymphocytes? The Spi evidence
Shintani, S., Terzić, J., Sato, A., Saraga‐Babić, M., Ó’hUigín, C., Tichy, H., & Klein, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110505597 · Cited by 80
PU.1 but not ets-2 is essential for macrophage development from embryonic stem cells
Henkel, G., McKercher, Sr., Yamamoto, H., Anderson, K., Oshima, R., & Maki, R. (1996) · Blood · doi:10.1182/blood.v88.8.2917.bloodjournal8882917 · Cited by 76
Self-citationRoss, I. L., Xie, Y., Ostrowski, M. C., & Hume, D. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6662 · Cited by 79
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
Metadata
- Authors
- Pongubala, J., Van Beveren, C., Nagulapalli, S., Klemsz, M., McKercher, Maki, R., & Atchison, M.
- Affiliations
- University of Pennsylvania (US)
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Venue
- Science
- Published
- 1993-03-12
- Volume
- 259
- Issue
- 5101
- Pages
- 1622-1625
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2093339251
- Cited by
- 271
- References
- 23
- Citations by year
- 2026: 3 · 2025: 1 · 2023: 5 · 2022: 3 · 2021: 1 · 2020: 3 · 2018: 1 · 2017: 1 · 2015: 2 · 2013: 1 · 2012: 7
- FWCI
- 8.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA042909)
- National Institute of General Medical Sciences (R01GM042415)
- National Institute of Allergy and Infectious Diseases (R01AI030656)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- PU.1, protein phosphorylation, casein kinase 2, protein-protein interaction, transcriptional activation, transcriptional regulation
- MeSH terms
- Animals, B-Lymphocytes, Base Sequence, Cell Line, Cell Nucleus, DNA-Binding Proteins, Enhancer Elements, Genetic, Immunoglobulin kappa-Chains, Molecular Sequence Data, Phosphorylation, Plasmacytoma, Recombinant Proteins, Transcription Factors, Transcription, Genetic, Transfection, Tumor Cells, Cultured, Oligonucleotide Probes, Retroviridae Proteins, Oncogenic, Mutagenesis, Site-Directed
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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