Stimulation of macrophages by lipopolysaccharide alters the phosphorylation state, conformation, and function of PU.1 via activation of casein kinase II
Abstract
We previously reported that LPS stimulation of the RAW264.7 murine macrophage cell line rapidly induced a structural change within the N terminus of the transcriptional regulatory factor PU.1. PU.1 is required for the expression of a variety of cytokine, cytokine receptor, and integrin genes. Western blot analysis of nuclear extracts prepared from LPS-stimulated macrophages revealed increased phosphorylation of PU.1 at serine residues relative to that in unstimulated controls. PU.1-DNA complexes prepared using nuclear extracts from LPS-stimulated macrophages were less sensitive to protease digestion compared with PU.1-DNA complexes generated using nuclear extracts prepared from unstimulated cells. This altered protease sensitivity probably reflects a conformational change within PU.1 resulting from LPS-induced phosphorylation. This possibility was supported by the finding that in vitro-phosphorylated PU.1 was similarly resistant to protease digestion. Transient transfection studies suggest that LPS-induced phosphorylation of PU.1 at serine 148, located within a casein kinase II (CKII) consensus motif, increases the transactivation function of PU.1. Other serine/CKII sites located at positions 41, 45, 132, and 133 do not appear to be required for LPS-induced PU.1 function. Lastly, we found that LPS also increased the enzymatic activity of CKII in these cells. To our knowledge, these are the first studies to demonstrate that LPS can stimulate CKII activity, induce PU.1 phosphorylation, and enhance the capacity of PU.1 to activate transcription in macrophages.
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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 [65]
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 [65]
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 [65]
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 148 phosphorylation is required for the lipopolysaccharide-induced transactivation function of PU.1.
“The serine 148 phosphorylation was also found to be required for the lipopolysaccharide-induced transactivation function of PU.1 (27).”
Activation of EICE-dependent transcription appears to involve phosphorylation of PU.1 as well as ICSBP.
“Activation of EICE-dependent transcription appears to involve phosphorylation of PU.1 as well as ICSBP (28, 45).”
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 [28]
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“…PU.1 protein by phosphorylation is a major avenue for exerting regulatory control of PU.1–DNA complex formation and PU.1–protein interactions occurring as a consequence of promoter-specific programming during myeloid differentiation (Rosmarin et al., 1995; Carey et al., 1996; Lodie et al., 1997).”
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Murine Protein Kinase CK2α′: cDNA and Genomic Cloning and Chromosomal Mapping
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E2a/Pbx1 oncogene inhibits terminal differentiation but not myeloid potential of pro-T cells
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“1 is potentially phosphorylated on five separate serine residues (Ser(41), Ser(45), Ser(132), Ser(133), and Ser(148)) and is an in vitro substrate for casein kinase II (CKII)(3) (5).”
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“1 through phosphorylation-mediated modifications (34, 35).”
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Structure and Activity of Endotoxins
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“Lodie et al. (Lodie et al., 1997) revealed that lipopolysaccharide stimulation induces phosphorylation of PU.1 at Ser148 (Figure 1), located within a CKII consensus motif, which increases the transactivation www.intechopen.com Myeloid Leukemia – Basic Mechanisms of Leukemogenesis 250 www.intechopen.com PU.1, a Versati…”
BackgroundInfluential
- Authors
- Lodie, T. A., Savedra, R., Golenbock, D. T., Van Beveren, C. P., Maki, R. A., & Fenton, M. J.
- Affiliations
- Boston University (US)
- Pulmonary Center, Boston University School of Medicine , MA 02118,
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 1997-02
- Volume
- 158
- Issue
- 4
- Pages
- 1848-1856
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2109572507
- Cited by
- 110
- References
- 0
- Citations by year
- 2026: 1 · 2024: 1 · 2022: 2 · 2020: 1 · 2019: 1 · 2018: 2 · 2016: 1 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 1
- FWCI
- 5.30
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- PU.1, casein kinase 2, lipopolysaccharide, macrophages, serine phosphorylation, protein conformation, transcriptional activation, transcription factor regulation
- MeSH terms
- Proto-Oncogene Protein Spi-1, Animals, Cell Line, Codon, DNA-Binding Proteins, Enzyme Activation, Humans
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