Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.

Eisenbeis, C F; Singh, H; Storb, U

doi:10.1101/gad.9.11.1377

PreprintCited by 447Genomics and Chromatin Dynamicsinterferon and immune responsesT-cell and B-cell Immunology

Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.

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Eisenbeis, C F, Singh, H, Storb, U·1995·Genes & Development

DOI 10.1101/gad.9.11.1377

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Abstract

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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Ectopic co-expression of PU.1 and Pip synergistically activates a reporter containing multiple copies of the IgL lambda composite element E lambda 2-4.
“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
Prior studies report that physical interaction between transcription factors can enhance DNA binding, which may explain synergy when two factors are present.
“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]
The PU.1- and Pip-binding sites in the λB composite element were identified by methylation interference analysis.
“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
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 [46]
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.
“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]

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“with the B cell-specific factor NF-EM5 (Pip) (8, 24).”
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Pip, a lymphoid-restricted IRF, contains a regulatory domain that is important for autoinhibition and ternary complex formation with the Ets factor PU.1.
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PU.1 recruits a second nuclear factor to a site important for immunoglobulin kappa 3' enhancer activity.
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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
DOI: 10.1101/gad.9.11.1377
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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Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.

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