A Two-Step Mechanism for Recruitment of Pip by PU.1

Perkel, Jeffrey M; Atchison, Michael L

doi:10.4049/jimmunol.160.1.241

Cited by 77Genomics and Chromatin DynamicsT-cell and B-cell ImmunologyDevelopmental Biology and Gene Regulation

A Two-Step Mechanism for Recruitment of Pip by PU.1

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Perkel, Jeffrey M, Atchison, Michael L·1998·The Journal of Immunology

DOI 10.4049/jimmunol.160.1.241

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Abstract

Transcription of the Ig κ light chain gene is controlled in part by the 3′ κ enhancer. Two of the proteins that bind to the 3′ enhancer, PU.1 and Pip, show tissue-restricted expression and may be responsible for the tissue specificity of 3′ enhancer activity. PU.1 alone can bind to DNA; however, Pip cannot bind to its 3′ enhancer site in electrophoretic mobility shift assays, unless recruited by PU.1. Previously, we showed that the PU.1 PEST domain (rich in the amino acids proline, glutamate, serine, and threonine; sequences 118–160) is necessary for Pip recruitment to DNA. Here we used detailed mutagenic analyzes of PU.1 to more precisely identify sequences required for Pip recruitment by electrophoretic mobility shift assay. We found that mutation of three segments within the PU.1 PEST domain (118–125, 133–139, and 141–147) modulated the efficiency of Pip recruitment, while mutation of sequences between residues 88–118 and 154–168 had no effect. Interestingly, we found that the PU.1 ETS domain (residues 170 to 255) is both necessary and sufficient for Pip interaction in solution and that other ETS domain proteins can physically interact with Pip as well. Our results suggest that Pip recruitment to DNA by PU.1 occurs via a two-step mechanism. First, a physical interaction that is not sufficient to recruit Pip occurs via the PU.1 ETS domain. Second, a conformational change in the PU.1 PEST domain, apparently mediated by serine phosphorylation, induces a conformational change in Pip enabling it to bind to DNA. We also show that the PU.1 PEST domain does not target PU.1 for rapid turnover.

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PU.1 forms complexes with IRF-4 and IRF-8 to drive cofactor-dependent expression, such as Toll-like receptor 4.
“Notably, besides transcription of genes that is directly dependent on PU.1mediated transactivation, PU.1 is also able to form complexes with cofactors as IRF-4 and IRF-8 to induce cofactordependent expression, for example, of Toll-like receptor 4 [50][51][52].”
From PKCδ-Induced PU.1 Phosphorylation Promotes Hematopoietic Stem Cell Differentiation to Dendritic Cells (2011) · cites this paper as [52]
The paper's Abstract (page not provided) identifies Pip as IRF4 and describes its recruitment by PU.1 to immunoglobulin enhancer DNA-binding sites. The passages support PU.1–IRF4 cooperation, but do not address PU.1 complexes with IRF8 or cofactor-dependent expression of Toll-like receptor 4. (LLM, conf=0.88)
Experimental — accuracy not yet measured
A recent study suggests PU.1 and Pip can interact in the absence of template DNA.
“A recent study using protein-protein interaction assays suggests that PU.1 and Pip can interact in the absence of template DNA”
From Assembly requirements of PU.1–Pip (IRF‐4) activator complexes: inhibiting function in vivo using fused dimers (1999) · cites this paper as Perkel et al., 1998
In the two-step recruitment mechanism for PU.1/Pip ternary complex, PU.1/Pip interaction is DNA template-directed and involves two distinct protein-protein interaction surfaces: (i) the ETS (PU.1) and IRF (Pip) DNA binding domains and (ii) the phosphorylated PEST domain of PU.1 and a putative α helix in Pip.
“A model was proposed for PU.1/Pip ternary complex. In this two-step recruitment mechanism, PU.1/Pip interaction is DNA template-directed and involves two distinct protein–protein interaction surfaces: (i) the ETS (PU.1) and IRF (Pip) DNA binding domains and (ii) the phosphorylated PEST domain of PU.1 and a putative α helix in Pip [118, 119] (Fig. 9).”
From PU.1 and partners: regulation of haematopoietic stem cell fate in normal and malignant haematopoiesis (2009) · cites this paper as [118]
The PU.1-ICSBP interaction is DNA directed and facilitated by EICE.
“Analogous to the PU.1-Pip interaction, the PU.1-ICSBP interaction is DNA directed and facilitated by EICE (4, 38).”
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 [38]
The PU.1-ICSBP interaction is dependent on the IAD domain in the C-terminal region, although the DBD is also required.
“the PU.1-ICSBP interaction is dependent on the IAD domain in the C-terminal region, although the DBD is also required for this interaction (5, 38).”
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 [38]

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Analysis of the physical interactions between PU.1 and Pip, two immunoglobulin kappa 3' enhancer binding proteins
Perkel, J. M. (1997) · Scholarly Commons (University of Pennsylvania)
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Analysis of the physical interactions between PU.1 and Pip, two immunoglobulin {\it kappa/} 3$\sp\prime$ enhancer-binding proteins
Perkel, J. M. (1997)
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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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PU.1 Recruits a Second Nuclear Factor to a Site Important for Immunoglobulin κ 3' Enhancer Activity
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Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator.
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Authors: Perkel, J. M., & Atchison, M. L.
Affiliations: University of Pennsylvania (US)
ORCID: Perkel, Jeffrey M
Venue: The Journal of Immunology
Publisher: Oxford University Press (OUP)
Published: 1998-01-01
Volume: 160
Issue: 1
Pages: 241-252
ISSN: 0022-1767 (ISSN-L)
1550-6606
DOI: 10.4049/jimmunol.160.1.241
OpenAlex: W1543294597
Cited by: 77
References: 43
Citations by year: 2025: 1 · 2024: 1 · 2022: 1 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 2 · 2015: 1 · 2012: 4
FWCI: 2.56
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: academic.oup.com/pages/standard-publication-reuse-rights (vor)
Locations: The Journal of Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM-42415, R01GM042415)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Keywords: PU.1, Pip, transcriptional regulation, protein-protein interaction, PEST domain, ETS domain, serine phosphorylation, protein conformational change, DNA binding, protein turnover, tissue specificity
MeSH terms: Proto-Oncogene Protein Spi-1, Amino Acid Sequence, Animals, Bacterial Proteins, Binding Sites, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Immunoglobulin kappa-Chains, Membrane Proteins, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Proto-Oncogene Proteins, Transcription Factors, Trans-Activators, 3T3 Cells, Proto-Oncogene Proteins c-ets, Mice

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A Two-Step Mechanism for Recruitment of Pip by PU.1

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