The DOI matches its Crossref record; 57 of the 58 references it cites were found in a registry or an index.
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
The cited source says what the claim attributes to it.
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]
The cited source says what the claim attributes to it.
In the citing paper
“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 cited source says what the claim attributes to it.
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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