ArticleMolecular and cellular biology1998
Transcription factor Pip can enhance DNA binding by E47, leading to transcriptional synergy involving multiple protein domains.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 65 citations in OpenAlex.
- The Roles of IRF-8 in Regulating IL-9-Mediated Immunologic Mechanisms in the Development of DLBCL: A State-of-the-Art Literature Review.Frontiers in oncology · 2022Review
- Helix-Loop-Helix Proteins in Adaptive Immune Development.Frontiers in immunology · 2022Review
- A Synchronous IRF4-Dependent Gene Regulatory Network in B and Helper T Cells Orchestrating the Antibody Response.Trends in immunology · 2020Review
- Transcription factors IRF8 and PU.1 are required for follicular B cell development and BCL6-driven germinal center responses.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Aberrant expression of ETS1 and ETS2 proteins in cancer.Cancer reports and reviews · 2018Article
- Spurious transcription factor binding: non-functional or genetically redundant?BioEssays : news and reviews in molecular, cellular and developmental biology · 2014Article
- A developmentally controlled competitive STAT5-PU.1 DNA binding mechanism regulates activity of the Ig κ E3' enhancer.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- PU.1 can recruit BCL6 to DNA to repress gene expression in germinal center B cells.Molecular and cellular biology · 2009Article
- IRF4: Immunity. Malignancy! Therapy?Clinical cancer research : an official journal of the American Association for Cancer Research · 2009Review
- E and ID proteins branch out.Nature reviews. Immunology · 2009Review
- IRF8 regulates myeloid and B lymphoid lineage diversification.Immunologic research · 2009Review
- Article
- Interferon regulatory factor 4 differentially regulates the production of Th2 cytokines in naive vs. effector/memory CD4+ T cells.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Interferon regulatory factor 4 and 8 in B-cell development.Trends in immunology · 2008Review
- A role for interferon regulatory factor 4 in receptor editing.Molecular and cellular biology · 2008Article
- Article
- B-cell receptor activation inhibits AID expression through calmodulin inhibition of E-proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Epigenetic histone modifications do not control Igkappa locus contraction and intranuclear localization in cells with dual B cell-macrophage potential.Journal of immunology (Baltimore, Md. : 1950) · 2006Article
- E2A and IRF-4/Pip promote chromatin modification and transcription of the immunoglobulin kappa locus in pre-B cells.Molecular and cellular biology · 2006Article
- Regulation of the germinal center gene program by interferon (IFN) regulatory factor 8/IFN consensus sequence-binding protein.The Journal of experimental medicine · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The transcription factors E2A (E12/E47) and Pip are both required for normal B-cell development. Each protein binds to regulatory sequences within various immunoglobulin enhancer elements. Activity of E2A proteins can be regulated by interactions with other proteins which influence their DNA binding or activation potential. Similarly, Pip function can be influenced by interaction with the protein PU.1, which can recruit Pip to bind to DNA. We show here that a previously unidentified Pip binding site resides adjacent to the E2A binding site within the immunoglobulin kappa 3' enhancer. Both of these binding sites are crucial for high-level enhancer activity. We found that E47 and Pip can functionally interact to generate a very potent 100-fold transcriptional synergy. Through a series of mutagenesis experiments, we identified the Pip sequences necessary for transcriptional activation and for synergy with E47. Two synergy domains (residues 140 to 207 and 300 to 420) in addition to the Pip DNA binding domain (residues 1 to 134) are required for maximal synergy with E47. We also identified a Pip domain (residues 207 to 300) that appears to mask Pip transactivation potential. Part of the synergy mechanism between E47 and Pip appears to involve the ability of Pip to increase DNA binding by E47, perhaps by inducing a conformational change in the E47 protein. E47 may also induce a conformational change in Pip which unmasks sequences important for transcriptional activity. Based upon our results, we propose a model for E47-Pip transcriptional synergy.
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