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Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.
Open accessAbstract
The immunoglobulin light-chain gene enhancers E kappa 3', E lambda 2-4, and E lambda 3-1 contain a conserved cell type-specific composite element essential for their activities. This element binds a B cell-specific heterodimeric protein complex that consists of the Ets family member PU.1 and a second factor (NF-EM5), whose participation in the formation of the complex is dependent on the presence of DNA-bound PU.1. In this report we describe the cloning and characterization of Pip (PU.1 interaction partner), a lymphoid-specific protein that is most likely NF-EM5. As expected, the Pip protein binds the composite element only in the presence of PU.1; furthermore, the formation of this ternary complex is critically dependent on phosphorylation of PU.1 at serine-148. The Pip gene is expressed specifically in lymphoid tissues in both B- and T-cell lines. When coexpressed in NIH-3T3 cells, Pip and PU.1 function as mutually dependent transcription activators of the composite element. The amino-terminal DNA-binding domain of Pip exhibits a high degree of homology to the DNA-binding domains of members of the interferon regulatory factor (IRF) family, which includes IRF-1, IRF-2, ICSBP, and ISGF3 gamma.
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“When co-expressed ectopically, PU.1 and Pip synergistically activate transcription of a reporter gene containing multiple copies of the composite element from the IgL λ enhancer, E λ2-4 (Eisenbeis et al., 1995).”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Eisenbeis et al., 1995
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In the citing paper
“In several studies, the physical interaction between transcription factors increases DNA-binding ability, providing an explanation for synergistic activation in the presence of two factors (11,18,56,58,67).”
From Multiple Functional Domains of AML1: PU.1 and C/EBPα Synergize with Different Regions of AML1 (1998) · cites this paper as [11]
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“The PU.1-and Pip-binding sites have been underlined based on methylation interference analysis of the λB site(Eisenbeis et al., 1995).”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Eisenbeis et al., 1995
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In the citing paper
“PIP is expressed exclusively in the lymphoid lineages (27”
From AKT Induces Transcriptional Activity of PU.1 through Phosphorylation-mediated Modifications within Its Transactivation Domain (2001) · cites this paper as [32]
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 [46]
In the citing paper
“Another highly homologous IRF family member, IRF-8/ICSBP, competes with Pip/IRF-4 for binding to PU.1 on the enhancer element and thus represses the transactivation activity of the complex [46].”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [46]
In the citing paper
“IRF-4 is similar to ICSBP in structure, interacts with some common partners (PU.1 and E47), and regulates an overlapping set of target promoters. (31,32,63,64)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [31]
In the citing paper
“IRF-4 is similar to ICSBP in structure, interacts with some common partners (PU.1 and E47), and regulates an overlapping set of target promoters. (31,32,63,64)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [31]
In the citing paper
“IRF-4 is similar to ICSBP in structure, interacts with some common partners (PU.1 and E47), and regulates an overlapping set of target promoters. (31,32,63,64)”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [31]
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Metadata
- Authors
- Eisenbeis, C. F., Singh, H., & Storb, U.
- Affiliations
- University of Chicago (US)
- ORCID
- Singh, H
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1995-06-01
- Volume
- 9
- Issue
- 11
- Pages
- 1377-1387
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2055192078
- Cited by
- 447
- References
- 58
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 4 · 2023: 7 · 2022: 9 · 2021: 7 · 2020: 12 · 2019: 3 · 2018: 4 · 2017: 6 · 2016: 8 · 2015: 6 · 2014: 11 · 2013: 17 · 2012: 15
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- American Cancer Society
- Arthritis Foundation
- National Institutes of Health
- U.S. Public Health Service (FM07183)
- National Institute of General Medical Sciences (T32GM007281, GM-07281)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Keywords
- Pip, PU.1, composite components, transcriptional activation, ternary protein complex, B cells, T cells
- MeSH terms
- Interferon Regulatory Factor-4, Amino Acid Sequence, Base Sequence, Cell Line, Cloning, Molecular, DNA-Binding Proteins, Gene Expression Regulation, Humans, Lymphocytes, Molecular Sequence Data, Transcription Factors, Trans-Activators, Retroviridae Proteins, Oncogenic, Sequence Alignment, Interferon Regulatory Factors
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