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
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[42] Detection and quantification of phosphotyrosine in proteins
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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
Cited by
Sorted by citations
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
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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