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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Pip binding to DNA requires DNA-bound PU.1 phosphorylated at Ser148.
“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
PU.1 can be phosphorylated by casein kinase or JNK in vitro.
“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]
Phosphorylation of PU.1 at Ser-148 is necessary for interaction with NF-EM5 or stimulation by lipopolysaccharide.
“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]
The activity of PU.1 is known to be regulated by phosphorylation.
“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]
Casein kinase II has been suggested to be responsible for phosphorylation of PU.1 at serine 148.
“casein kinase II has been suggested to be responsible for phosphorylation of PU.1 at serine 148 (27, 35)”
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).
“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).”
Phosphorylation of PU.1 at serine 148 is required for its interaction with PIP (NF-EM5) and activates the immunoglobulin κ 3′ enhancer.
“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).”
PU.1 is a phosphoprotein.
“PU.1 is a phosphoprotein”
The PEST domain interacts with IRFs including Pip/NF-EM5 and ICSBP.
“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]
Similar ICSBP protein-protein interactions are necessary for activation of the TOLL-like receptor 4 gene in mature monocytes.
“Similar ICSBP protein-protein interactions are necessary for activation of the TOLL-like receptor 4 gene in mature monocytes (22).”
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“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., Mathieu, C., & Ezekowitz, R. A. B. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.179.6.1985 · Cited by 119 · see citing works
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 · see citing works
“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 · see citing works
Fletcher, J. C., & Thummel, C. S. (1995) · Development · doi:10.1242/dev.121.5.1411 · Cited by 113 · see citing works
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 112 · see citing works
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 111 · see citing works
“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 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 101 · see citing works
Zhao, B., & Sample, C. E. (2000) · Journal of Virology · doi:10.1128/jvi.74.11.5151-5160.2000 · Cited by 104 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
“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 98 · see citing works
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 · see citing works
“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 · see citing works
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 96 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
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 · see citing works
Yamada, T., Kondoh, N., Matsumoto, M., Yoshida, M., Maekawa, A., & Oikawa, T. (1997) · Blood · doi:10.1182/blood.v89.4.1383 · Cited by 91 · see citing works
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 · see citing works
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 · see citing works
“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).”
BackgroundPerez, 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 · see citing works
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 · see citing works
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 · see citing works
Self-citationMarecki, S., Atchison, M. L., & Fenton, M. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.5.2713 · Cited by 87 · see citing works
Self-citationStütz, A. M., & Woisetschläger, M. (1999) · PubMed · Cited by 86 · see citing works
Himmelmann, A. W., Riva, A., Wilson, G. L., Lucas, B. P., Thévenin, C., & Kehrl, J. H. (1997) · Blood · doi:10.1182/blood.v90.10.3984 · Cited by 84 · see citing works
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
“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 · see citing works
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 81 · see citing works
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 · see citing works
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 78 · see citing works
- 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
- 282
- References
- 23
- Citations by year
- 2026: 2 · 2025: 1 · 2023: 4 · 2022: 4 · 2021: 1 · 2020: 2 · 2018: 1 · 2017: 1 · 2015: 2 · 2013: 1 · 2012: 7
- FWCI
- 10.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- 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
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