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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Items 201–276 of 276
Gunther, C. V., & Graves, B. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7569-7580.1994 · Cited by 24
“1 interacts with NF-EM5 on the immunoglobulin K-chain 3' enhancer (35).”
BackgroundMutants of ETS domain PU.1 and GGAA/T recognition: Free energies and kinetics
Pio, F., Assa‐Munt, N., Yguerabide, J., & Maki, R. A. (1999) · Protein Science · doi:10.1110/ps.8.10.2098 · Cited by 22
“Some ternary complexes composed of PU.1 or ETS-1 with other transcription factors binding to adjacent sites have been characterized ~Pongubala et al., 1992, 1993; Brass et al., 1996; Erman & Sen, 1996; Nikolajczyk et al., 1996!. Recently, the first crystal structure of the ETS domain of PU.1…”
BackgroundSelf-citationCritical Functions of IRF4 in B and T Lymphocytes
Hagman, J. R. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1701385 · Cited by 22
“1’s specific phosphorylation by casein kinase II (3).”
BackgroundKasibhatla, S., Tailor, P., Bonnefoy, N., Mustelin, T., Altman, A., & Fotedar, A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.2021 · Cited by 22
“The GST–c-Jun (1-223) vector was obtained from M.”
BackgroundMethodInfluentialPU.1-mediated Transcription Is Enhanced by HMG-I(Y)-dependent Structural Mechanisms
Lewis, R. T., Andreucci, A., & Nikolajczyk, B. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008726200 · Cited by 22
PU.1 is required for transcriptional activation of the Stat6 response element in the Igϵ promoter
Pesu, M., Aittomäki, S., Välineva, T., & Silvennoinen, O. (2003) · European Journal of Immunology · doi:10.1002/eji.200323680 · Cited by 22
Nimer, S. D., Zhang, W., Kwan, K. W., Whang, Y. E., Zhang, J., & Whang, Y. W. Y. C. T. (1996) · Blood · doi:10.1182/blood.v87.9.3694.bloodjournal8793694 · Cited by 21
HMGA1 Co-activates Transcription in B Cells through Indirect Association with DNA
McCarthy, K. M., McDevit, D. C., Andreucci, A., Reeves, R., & Nikolajczyk, B. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308586200 · Cited by 22
Nagulapalli, S., Goheer, A., Pitt, L. K., McIntosh, L. P., & Atchison, M. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7337-7350.2002 · Cited by 20
Self-citationBreig, O., Théoleyre, O., Douablin, A., & Baklouti, F. (2010) · Oncogene · doi:10.1038/onc.2010.29 · Cited by 19
“1 is phosphorylated on multiple serine residues in its transactivation and PEST regions (Pongubala et al., 1993).”
BackgroundLiu, X., Prabhu, A., & Ness, B. V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3285 · Cited by 19
Hines, R., Sorensen, B. R., Shea, M. A., & Maury, W. J. (2004) · Journal of Virology · doi:10.1128/jvi.78.7.3407-3418.2004 · Cited by 19
“1/pET) vector plasmid (37) was inoculated into a”
MethodPub, 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
Carlsson, R., Persson, C., & Leanderson, T. (2003) · Molecular Immunology · doi:10.1016/s0161-5890(03)00032-4 · Cited by 18
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
“For example, Igk activation is dependent on phosphorylation of Ser148 on PU.1 and interaction with IRF-4, while induction of myeloid differentiation is independent of Ser phosphorylation and the Ets domain, but involves the glutamine-rich transactivation domain of PU.1 ( 30 ,31).”
BackgroundPU.1 regulates the expression of the human neutrophil elastase gene
Srikanth, S., & Rado, T. A. (1998) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00039-6 · Cited by 18
Co-crystallization of an ETS Domain (PU.1) in Complex with DNA
Pio, F., Ni, C., Mitchell, R. S., Knight, J., McKercher, S. R., Klemsz, M. J., Lombardo, A. M., Maki, R. A., & Ely, K. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24258 · Cited by 17
Self-citationCrystallization and characterization of PU.1/IRF-4/DNA ternary complex
Escalante, C. R., Shen, L., Escalante, M. C., Brass, A. L., Edwards, T. A., Singh, H., & Aggarwal, A. K. (2002) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00514-2 · Cited by 17
Pyerin, W. G., Ackermann, K., & Lorenz, P. (1996) · doi:10.1002/9783527615032.ch4 · Cited by 17
Ikizawa, K., Kajiwara, K., Izuhara, K., & Yanagihara, Y. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5723 · Cited by 16
Curtiss, B. M., VanCampen, J., Macaraeg, J., Kong, G., Taherinasab, A., Tsuchiya, M., Yashar, W. M., Tsang, Y. H., Horton, W. R., Coleman, D. J., et al. (2022) · Leukemia · doi:10.1038/s41375-022-01594-1 · Cited by 14
“PU.1 is phosphorylated at Ser148 [42, 43] leading to increased activity and DNA binding.”
BackgroundJernberg‐Wiklund, H., & Nilsson, K. (2002) · Human cell culture · doi:10.1007/0-306-46877-8_4 · Cited by 16
Multiple Regulatory Elements Control the Basal Promoter Activity of the Human α4 Integrin Gene
AUDET, J.-F., Masson, J., Rosen, G., Salesse, C., & Guérin, S. L. (1994) · DNA and Cell Biology · doi:10.1089/dna.1994.13.1071 · Cited by 15
“Recently, PU.l, a member of the Ets family of transcription factors, was shown to recruit, through proteinprotein interactions, the binding of a second B-cell-re-stricted nuclear factor, designated NF-EM5, in the 3' enhancer of the immunoglobulin k gene (Pongubala et al., 1992, 1993).”
Heydemann, A., Boehmler, J. H., & Simon, M. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29527 · Cited by 15
Conrad, K. E., Oberwetter, J. M., Vaillancourt, R., et al. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1553-1565.1994 · Cited by 16
“1, an Ets member, and NF-EM5, a Blymphocyte cell-specific transcription factor, which has been shown to be required for optimal transcription activation of the immunoglobulin K 3' enhancer (54); (ii) a 10-bp domain containing an Ets- and LyF-1-binding site that is required for the B- and T-lymphocyte-restricted expres…”
BackgroundLiu, H., Duan, Z., Zheng, H., Hu, D., Li, M., Tao, Y., Bode, A. M., Dong, Z., & Cao, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032624 · Cited by 15
“1 [17].”
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
The regulation of GM-CSF is dependent on a complex interplay of multiple nuclear proteins
Kaushansky, K., O'Rork, C., Shoemaker, S. G., et al. (1996) · Molecular Immunology · doi:10.1016/0161-5890(95)00156-5 · Cited by 15
McKercher, S. R., Lombardo, C. R., Bobkov, A. A., Jia, X., & Assa‐Munt, N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0136910100 · Cited by 14
Azim, A. C., Wang, X., Park, G. Y., Sadikot, R. T., Cao, H., Mathew, B., Atchison, M., van Breemen, R. B., Joo, M., & Christman, J. W. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7868 · Cited by 17
“PU.1 interacts with many transcription factors, including IFN regulatory factor 4 (NF-EM5/PIP, c-JUN, and GATA-1 (9, 32), to result in combinatorial transcriptional regulation of gene expression.”
BackgroundInfluentialSelf-citationKihara-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 15
The murine AIDS defective provirus acts as an insertional mutagen in its infected target B cells
Huang, M., Takáč, M., Kozak, C. A., & Jolicoeur, P. (1995) · Journal of Virology · doi:10.1128/jvi.69.7.4069-4078.1995 · Cited by 13
“The activity of this protein on transcription is regulated by phosphorylation (50).”
BackgroundDNA binding and transcription activation by chicken interferon regulatory factor-3 (chIRF-3)
Grant, C. E. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.23.4790 · Cited by 12
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
Regulation of immunoglobulin gene transcription
Calame, K. L., & Ghosh, S. (1995) · Elsevier eBooks · doi:10.1016/b978-012053640-5/50021-5 · Cited by 12
Kim, J., Ogata, Y., Ali, H., & Feldman, R. A. (2004) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2003.12.004 · Cited by 11
Hodawadekar, S., Park, K., Farrar, M. A., & Atchison, M. L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102239 · Cited by 10
“1 DNA binding at the kE39 enhancer functions to nucleate binding of other enhancer factors (16, 31, 39).”
BackgroundSelf-citationNakano, N., Nishiyama, C., Masuoka, N., Nishiyama, M., Yamane, H., Okumura, K., & Ogawa, H. (2005) · Immunogenetics · doi:10.1007/s00251-004-0754-2 · Cited by 11
“…interaction between human PU.1 and human IRF-4, a double mutant S132/133A (S131/132A of rat PU.1) interacted with IRF-4 to a considerably low extent (Pongubala et al. 1993), and mutation of sequences 133–139 (132–138 of rat PU.1) dramatically reduced IRF-4 recruitment (Perkel and Atchison 1998).”
BackgroundThe 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.14.4.2604-2615.1994 · Cited by 11
“significant modifications in the intensity of the BA-1 and MS-1 complexes, reflecting perhaps transcriptional and/or posttranslational modifications that may contribute to the phorbol ester response as has been shown for other Ets factors (18, 31, 43).”
BackgroundCasein kinase-2 and cell signaling
Pinna, L. A., Meggio, F., & Sarno, S. (1995) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-9057-1_2 · Cited by 11
Kao, S., Miyagi, E., Mallorson, R., Saito, H., Sukegawa, S., Mukherji, A., Mateja, A., Ferhadian, D., Fabryova, H., Clouse, K., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00652-22 · Cited by 8
“In particular, the interaction of PU.1 with another B cell-restricted nuclear factor, EM5, was shown to be dependent on PU.1 phosphorylation at Ser148 (24).”
BackgroundInfluentialKwok, J. C., Perdomo, J., & Chong, B. H. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21264 · Cited by 9
“…a role in transactivation (aa1–100) [Klemsz and Maki, 1996]; the PEST domain in the middle that is important for protein-protein interaction (aa116–170) [Rogers et al., 1986; Pongubala et al., 1993]; and the Ets domain at the C-terminus that is involved in DNA-binding activity (aa171–257) (Fig.”
BackgroundCasein kinase II in signal transduction and cell cycle regulation
Litchfield, D. W., & Lüscher, B. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2600-1_18 · Cited by 9
SPI-1 transforming properties depend upon specifically activated forms of the EPOR
Pereira, R. M., Raingeaud, J., Pironin, M., Ghysdael, J., & Quang, C. T. (2000) · Oncogene · doi:10.1038/sj.onc.1203886 · Cited by 10
“Direct e ects could involve the regulation of SPI-1 phosphorylation either on identi®ed sites (Pongubala et al., 1993) or on novel residues in domains critical for its activity.”
BackgroundPhosphorylation of the Spi‐B transcription factor reduces its intrinsic stability
Ray-Gallet, D., & Moreau-Gachelin, F. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01687-7 · Cited by 7
Hodawadekar, S., Wei, F., Yu, D., Thomas‐Tikhonenko, A., & Atchison, M. L. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.9.6165 · Cited by 7
Self-citationIshii, H., Sen, R., & Pazin, M. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308973200 · Cited by 6
Herwig, S., Su, Q., & Tempst, P. (1998) · Leukemia Research · doi:10.1016/s0145-2126(98)00086-1 · Cited by 6
Evidence against requirement of Ser41 and Ser45 for function of PU.1 – Molecular cloning of rat PU.1
Nishiyama, C., Masuoka, N., Nishiyama, M., Ito, T., Yamane, H., Okumura, K., & Ogawa, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.008 · Cited by 5
Rhodes, S. D., Yang, H., Dong, R., Menon, K., He, Y., Li, Z., Shi, C., Staser, K. W., Jiang, L., Wu, X., et al. (2015) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2538 · Cited by 6
“1 plays a central role in modulating its DNA binding affinity,((37,46)) and is thereby critical to its ability to activate myeloid-specific gene programs that promote terminal differentiation.”
BackgroundInsights into the transcriptional regulation of CD22 in B cell chronic lymphocytic leukemia
Enkhbayar, B., Lu, S., Tsai, H.-Y., Liang, S., Wu, S., Lin, K., & Angata, T. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108386 · Cited by 4
“It is recruited to a composite motif called the ETS-IRF composite element (EICE; consensus: 5 0 -GGAANNGAAA-3 0 (N: any nucleotide) (43)) that is occupied by PU.1 (44, 45) or Spi-B (46).”
Xie, Y., Ross, I. L., Browne, C. M., Lichanska, A. M., Favot, P., Ostrowski, M. C., & Hume, D. A. (1996) · Immunobiology · doi:10.1016/s0171-2985(96)80016-7 · Cited by 4
Curtiss, B. M., VanCampen, J., Kong, G., Yashar, W. M., Tsang, Y. H., Horton, W. R., Coleman, D. J., Estabrook, J., Lusardi, T. A., Mills, G. B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.24.456354 · Cited by 3
Gao, Z., Smith, A., Scott, J. N. F., Bevington, S. L., & Boyes, J. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad741 · Cited by 2
“From this, and previous studies ( 24 , 39 , 40 ), it is feasible that PU.1 provides a binding platform for IRF4.”
BackgroundResultGao, Z., Wang, M., Smith, A., & Boyes, J. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168315 · Cited by 3
Regulation of cytokine transcription in the context of chromatin
Nikolajczyk, B. S. (2006) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-006-0037-8 · Cited by 3
“Because IRF-4 recruitment requires PU.1 phosphorylation [ 60 ], and cellular stimulation results in activation of a PU.1 kinase, CK2, we have proposed that phosphorylation of constitutively DNA-bound PU.1 is important for inducible IL-1β transcription.”
BackgroundType 1 interferon perturbates clonal competition by reshaping human blood development
Lama, C., Isakov, D., Rosenberg, S., Quijada-Álamo, M., Saurty-Seerunghen, M. S., Moein, S., Nozais, M., Abera, T.-A., Sakaguchi, O., Totwani, M., et al. (2026) · Nature Genetics · doi:10.1038/s41588-026-02751-3 · Cited by 3
Changes in immunoglobulin–nucleoprotein complex structure mapped by chromatin immunoprecipitation
McDevit, D. C., & Nikolajczyk, B. S. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2005.10.003 · Cited by 2
Type 1 interferon perturbates clonal competition by reshaping human blood developmentPreprint
Lama, C., Isakov, D., Rosenberg, S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.28.509751 · Cited by 2
Mallorson, R., Miyagi, E., Kao, S., Sukegawa, S., Saito, H., Fábryová, H., Ruggieri, L. M., Mediouni, S., Valente, S. T., & Strebel, K. (2023) · Journal of Virology · doi:10.1128/jvi.01702-23 · Cited by 1
“7) was required for its interaction with NF-EM5 protein and recruitment to the immunoglobulin κ 3 ′ enhancer complex (24).”
BackgroundThe Role of PU.1 in the Regulation of Lymphoid and Myeloid Hematopoietic Progenitors
Scott, E. W. (1998) · Humana Press eBooks · doi:10.1007/978-1-4757-2778-4_7 · Cited by 1
Mechanisms of Transcriptional Regulation
Marecki, S., & Fenton, M. J. (2000) · Cited by 2
ETS transcription factor knockouts: A review
Bassuk, A. G. (1999) · Clinical Immunology Newsletter · doi:10.1016/s0197-1859(00)89197-9
LaVallee, T. M., & Morrison, S. L. (1996) · Molecular Immunology · doi:10.1016/s0161-5890(96)00036-3
Expression and activation of STAT and IRF family transcription factors in mononuclear leukocytes
Lehtonen, A. (2005) · Työväentutkimus Vuosikirja
Real, D. (2013) · CaltechTHESIS (California Institute of Technology) · doi:10.7907/pews-km18
Regulation of osteoclast differentiation by transcription factors MITF, PU.1 and EOS.
Hu, R. (2007) · OhioLink ETD Center (Ohio Library and Information Network)
Kamath, M. B. (2009) · OhioLink ETD Center (Ohio Library and Information Network)
Hormonally Regulated Transcription Factors
Bolander, F. F. (1994) · Elsevier eBooks · doi:10.1016/b978-0-12-111231-8.50017-7
The role of PU.1 and IRF4 interaction in the biology and function of T helper 2 cells
Ahyi, A.-N. N. (2009) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1686
Brg1 regulates fibroblast-myofibroblast transition to promote renal fibrosisPreprint
Wu, X., Luo, Y., Kang, A., Ni, J., Kong, M., & Zhang, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.22.572996
10.1016/b978-1-4557-5414-4.00001-2
(2000) · Time to knit · doi:10.1016/b978-1-4557-5414-4.00001-2
Regulation of Neutrophil Proteinases
Sturrock, A., & Hoidal, J. R. (1999) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8831-8_6
Roos‐Weil, D. (2018) · theses.fr (ABES) · doi:10.70675/1030cb13z12b8z4f7cz8f8az165206a6209a
Ramani, M., Nguyen, N., Solis, J., Tenen, D. G., & Trinh, B. Q. (2026) · Biology · doi:10.3390/biology15181657
“This region interacts with cofactors such as CBP/p300, TFIID, and Mediator [12,37–40].”
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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